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Active sites of thioredoxin reductases: why selenoproteins?

Active sites of thioredoxin reductases: why selenoproteins?

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Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea Nematode selenoproteome: the use of the selenocysteine insertion system to decode one codon in an animal genome?Evolution of selenium utilization traits.Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases The molecular biology of selenocysteine Relaxation of Selective Constraints Causes Independent Selenoprotein Extinction in Insect Genomes Structural and Biochemical Studies Reveal Differences in the Catalytic Mechanisms of Mammalian and Drosophila melanogaster Thioredoxin Reductases †Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1 Differing views of the role of selenium in thioredoxin reductase NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.TrxR1 as a potent regulator of the Nrf2-Keap1 response system Selective targeting of selenocysteine in thioredoxin reductase by the half mustard 2-chloroethyl ethyl sulfide in lung epithelial cells Effects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome Lokiarchaeota Marks the Transition between the Archaeal and Eukaryotic Selenocysteine Encoding Systems Influence of pH and flanking serine on the redox potential of S-S and S-Se bridges of Cys-Cys and Cys-Sec peptides.Selenium in chemistry and biochemistry in comparison to sulfur.The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state.Sec-containing TrxR1 is essential for self-sufficiency of cells by control of glucose-derived H2O2.Redox active motifs in selenoproteins.Genes for selenium dependent and independent formate dehydrogenase in the gut microbial communities of three lower, wood-feeding termites and a wood-feeding roach.Cross-linking of thioredoxin reductase by the sulfur mustard analogue mechlorethamine (methylbis(2-chloroethyl)amine) in human lung epithelial cells and rat lung: selective inhibition of disulfide reduction but not redox cycling.Selenoproteins: molecular pathways and physiological roles.Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism.Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family Targeted insertion of cysteine by decoding UGA codons with mammalian selenocysteine machinery Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase.Characterization of protein targets of mammalian thioredoxin reductases.Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein.TGL-mediated lipolysis in Manduca sexta fat body: possible roles for lipoamide-dehydrogenase (LipDH) and high-density lipophorin (HDLp)Thioredoxin glutathione reductase: its role in redox biology and potential as a target for drugs against neglected diseases.Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage Genome Analysis of Planctomycetes Inhabiting Blades of the Red Alga Porphyra umbilicalis SelenoDB 1.0 : a database of selenoprotein genes, proteins and SECIS elements Selenocysteine in thiol/disulfide-like exchange reactions.Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni.Selenium in thioredoxin reductase: a mechanistic perspective.Investigation of the C-terminal redox center of high-Mr thioredoxin reductase by protein engineering and semisynthesis.Characterization of mitochondrial thioredoxin reductase from C. elegans Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes

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Active sites of thioredoxin reductases: why selenoproteins?

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Proceedings of the National Academy of Sciences of the United States of America

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Charles H Williams

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David P Ballou

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Holger Bauer

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L David Arscott

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Linda Johansson

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R Heiner Schirmer

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Susanne Rauch

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P2860

Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge

Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster

Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations

High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes

Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene

Molecular and cellular aspects of thiol-disulfide exchange.

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