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Selenocysteine Derivatives for Chemoselective Ligations
ChemBioChem, 2002AbstractFor Abstract see ChemInform Abstract in Full Text.
Matt D, Gieselman +4 more
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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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RNA binding proteins and selenocysteine
BioFactors, 2001AbstractSelenocysteine is incorporated into protein by a complex co‐translational mechanism that involves both cis and trans acting factors. Among the trans‐acting factors are RNA binding proteins that interact with the selenoprotein 3′ UTRs at a sequence known as the selenocysteine insertion sequence (SECIS). These factors are generally referred to as
P R, Copeland, D M, Driscoll
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Evolutionary Basis for the Use of Selenocysteine
2011Evolutionary adaptations to dietary selenium may explain the use of selenocysteine in proteins. If so, adaptive signals should be present in the genomic regions of selenoprotein genes. It is, however, difficult to identify the signatures of adaptation left by natural selection in the genome of extant species (including humans).
White, L. +1 more
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Occurrence and characterization of selenocysteine in proteins
1984Publisher Summary This chapter focuses on the occurrence and characterization of selenocysteine in proteins. Four selenium-dependent enzymes that contain essential selenium in the form of selenocysteine residues have been identified to date. Three of these are of bacterial origin—glycine reductase, certain formate dehydrogenases, and α hydrogenase ...
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Common modifications of selenocysteine in selenoproteins
Essays in Biochemistry, 2019Abstract Selenocysteine (Sec), the sulfur-to-selenium substituted variant of cysteine (Cys), is the defining entity of selenoproteins. These are naturally expressed in many diverse organisms and constitute a unique class of proteins.
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