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1. Full Text Natural and synthetic selenoproteins
by Metanis, Norman and Hilvert, Donald
Current Opinion in Chemical Biology, ISSN 1367-5931, 10/2014, Volume 22, pp. 27 - 34
Once considered highly toxic, the element selenium is now recognized as a micronutrient essential for human health. It is inserted co-translationally into many... 
EXPRESSED PROTEIN LIGATION | PEPTIDES | BIOPHYSICS | SMALL-MOLECULE DISELENIDES | PHYSIOLOGICAL ROLES | BIOCHEMISTRY & MOLECULAR BIOLOGY | NATIVE CHEMICAL LIGATION | GLUTATHIONE-PEROXIDASE | ESCHERICHIA-COLI | SULFOXIDE REDUCTASES | SELENOCYSTEINE INCORPORATION | SELENIUM | Recombinant Proteins - metabolism | Selenocysteine - metabolism | Protein Biosynthesis | Oxidation-Reduction | Selenoproteins - genetics | Humans | Selenocysteine - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Selenoproteins - chemical synthesis | Protein Folding | Selenoproteins - metabolism | Selenoproteins - chemistry | Animals | Recombinant Proteins - chemical synthesis | Selenocysteine - genetics | Selenocysteine - chemical synthesis | Proteins
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2. Full Text Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme
by Seale, Lucia A
Antioxidants (Basel, Switzerland), ISSN 2076-3921, 09/2019, Volume 8, Issue 9, p. 357
The enzyme selenocysteine β-lyase (SCLY) was first isolated in 1982 from pig livers, followed by its identification in bacteria. SCLY works as a homodimer,... 
selenocysteine lyase | selenium | selenocysteine
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3. Full Text Chemical characterisation and speciation of organic selenium in cultivated selenium-enriched Agaricus bisporus
by Maseko, Tebo and Callahan, Damien L and Dunshea, Frank R and Doronila, Augustine and Kolev, Spas D and Ng, Ken
Food Chemistry, ISSN 0308-8146, 12/2013, Volume 141, Issue 4, pp. 3681 - 3687
The selenium concentration in cultivated in growth compost irrigated with sodium selenite solution increased by 28- and 43-fold compared to the control... 
Selenocysteine | Agaricus bisporus | Selenium-enriched mushrooms | Selenoproteins | Methyl-selenocysteine | Selenomethionine | FOOD SCIENCE & TECHNOLOGY | COLON | CHROMATOGRAPHY | MILK-PROTEINS | YEAST | SE | NUTRITION & DIETETICS | SELENOPROTEIN | PLASMA-MASS SPECTROMETRY | LENTINULA-EDODES | SHIITAKE MUSHROOM | CHEMISTRY, APPLIED | EXPRESSION | Selenocysteine - metabolism | Selenomethionine - metabolism | Cystine - analysis | Organoselenium Compounds - analysis | Agaricus - growth & development | Agaricus - metabolism | Agaricus - chemistry | Selenomethionine - analysis | Selenium - metabolism | Selenocysteine - analysis | Selenium - analysis | Cystine - metabolism | Selenocysteine - analogs & derivatives | Cystine - analogs & derivatives | Organoselenium Compounds - metabolism | Proteins | Selenium
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4. Full Text Selenoproteins—What unique properties can arise with selenocysteine in place of cysteine?
by Arnér, Elias S.J
Experimental Cell Research, ISSN 0014-4827, 2010, Volume 316, Issue 8, pp. 1296 - 1303
The defining entity of a selenoprotein is the inclusion of at least one selenocysteine (Sec) residue in its sequence. Sec, the 21st naturally occurring... 
Selenocysteine | Selenoprotein | Cysteine | Reactivity | Nucleophilicity | CRYSTAL-STRUCTURE | ACTIVE-SITES | SULFUR | SELENIUM | MAMMALIAN THIOREDOXIN REDUCTASE | CELL BIOLOGY | ONCOLOGY | RECOMBINANT PROTEINS | RESIDUES | OXIDOREDUCTASES | Selenocysteine - metabolism | Selenoproteins - chemistry | Animals | Selenocysteine - genetics | Selenoproteins - genetics | Humans | Selenocysteine - chemistry | Cysteine - metabolism | Cysteine - chemistry | Selenoproteins - metabolism | Cysteine - genetics | Oxidases | Thiols | Chemical properties | Selenium | Cystine | Proteins | Enzymes | Amino acids | Catalysis | Cellular biology | REVIEWS | CATALYSIS | ELECTRON TRANSFER | CHEMICAL PROPERTIES | BIOSYNTHESIS | INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY | CHEMICAL REACTIONS | CYSTEINE | 60 APPLIED LIFE SCIENCES | REDOX POTENTIAL
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5. Full Text Mechanism and regulation of selenoprotein synthesis
by Driscoll, Donna M and Copeland, Paul R
Annual Review of Nutrition, ISSN 0199-9885, 2003, Volume 23, pp. 17 - 40
Selenium is an essential trace element that is incorporated into proteins as selenocysteine (See), the twenty-first amino acid. Sec is encoded by a UGA codon... 
Selenocysteine | SECIS | Translation | Termination | Selenium | termination | ESCHERICHIA-COLI | BINDING-PROTEIN | ELONGATION-FACTOR SELB | HYDROPEROXIDE GLUTATHIONE-PEROXIDASE | selenocysteine | RNA STRUCTURAL MOTIF | EUKARYOTIC TRANSLATION INITIATION | NUTRITION & DIETETICS | selenium | SELENOCYSTEINE INSERTION-SEQUENCE | MESSENGER-RNA | HAMSTER OVARY CELLS | FORMATE DEHYDROGENASE-H | translation | Proteins - physiology | Protein Biosynthesis | Selenocysteine - physiology | Animals | Codon | Selenocysteine - genetics | Humans | Selenocysteine - chemistry | Kinetics | Mutation | Selenoproteins
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6. Full Text Selenium in chemistry and biochemistry in comparison to sulfur
by Wessjohann, Ludger A and Schneider, Alex and Abbas, Muhammad and Brandt, Wolfgang
Biological Chemistry, ISSN 1431-6730, 10/2007, Volume 388, Issue 10, pp. 997 - 1006
What makes selenoenzymes - seen from a chemist's view - so special that they cannot be substituted by just more analogous or adapted sulfur proteins? This... 
Selenocysteine | Enzyme mechanisms | Synthesis | Disulfide/diselenide/selenenylsulfide interchange | Selenoproteins | synthesis | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-MAGNETIC-RESONANCE | GLUTATHIONE-PEROXIDASE | ESCHERICHIA-COLI | enzyme mechanisms | THIOREDOXIN REDUCTASE-ACTIVITY | disulfide/diselenide/selenenylsulfide interchange | DISULFIDE EXCHANGE-REACTIONS | selenocysteine | AMINO-ACID-SEQUENCE | SELENOCYSTEINE INSERTION-SEQUENCE | KNUDSEN CELL METHOD | FORMATE DEHYDROGENASE-H | selenoproteins | Glutathione Peroxidase - metabolism | Selenium - chemistry | Selenocysteine - metabolism | Sulfur - metabolism | Peptides - chemistry | Humans | Selenocysteine - chemistry | Formate Dehydrogenases - metabolism | Selenoproteins - metabolism | Selenoproteins - chemistry | Sulfhydryl Compounds - metabolism | Animals | Peptides - metabolism | Selenium - metabolism | Thioredoxin-Disulfide Reductase - metabolism | Selenocysteine - chemical synthesis | Sulfhydryl Compounds - chemistry | Kinetics | Hydrogen-Ion Concentration | Sulfur - chemistry | Thioredoxin-Disulfide Reductase - chemistry | Enzymes | Thiols | Peptides | Amino acids | Biochemistry | Selenium | Sulfur
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7. Full Text Which form is that? The importance of selenium speciation and metabolism in the prevention and treatment of disease
by Weekley, Claire M and Harris, Hugh H
Chemical Society Reviews, ISSN 0306-0012, 11/2013, Volume 42, Issue 23, pp. 887 - 8894
The biological activity of selenium is dependent upon its speciation. We aim to integrate selenium speciation and metabolism into a discussion of the... 
SODIUM SELENITE | PROTEIN-KINASE-C | BETA-ELIMINATION REACTIONS | INDUCED OXIDATIVE STRESS | PROSTATE-CANCER | GLUTATHIONE-PEROXIDASE ACTIVITY | LUNG-CANCER CELLS | CONTAINING AMINO-ACIDS | CHEMISTRY, MULTIDISCIPLINARY | THIOREDOXIN REDUCTASE-ACTIVITY | HPLC-ICP-MS | Selenocysteine - metabolism | Selenomethionine - metabolism | Reactive Oxygen Species - metabolism | Humans | Neoplasms - prevention & control | Selenium Compounds - metabolism | Clinical Trials as Topic | Histone Deacetylase Inhibitors - chemistry | Selenoproteins - metabolism | Selenomethionine - therapeutic use | Selenoproteins - chemistry | Cystine - metabolism | Cystine - therapeutic use | Sulfhydryl Compounds - chemistry | Selenocysteine - therapeutic use | Histone Deacetylase Inhibitors - metabolism | Selenocysteine - analogs & derivatives | Cystine - analogs & derivatives | Dietary Supplements | Selenium Compounds - therapeutic use | Organoselenium Compounds - metabolism | Organoselenium Compounds - therapeutic use | Selenium compounds | Pathways | Medical services | Selenium | Biological | Metabolism | Chemical compounds | Speciation
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8. Full Text Translational redefinition of UGA codons is regulated by selenium availability
by Howard, Michael T and Carlson, Bradley A and Anderson, Christine B and Hatfield, Dolph L
Journal of Biological Chemistry, ISSN 0021-9258, 07/2013, Volume 288, Issue 27, pp. 19401 - 19413
Incorporation of selenium into similar to 25 mammalian selenoproteins occurs by translational recoding whereby in-frame UGA codons are redefined to encode the... 
RAT-LIVER | MEDIATED DECAY | DIETARY SELENIUM | METHYLATION | SELENOPROTEIN | MESSENGER-RNA | SEQUENCES | SELENOCYSTEINE TRANSFER-RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | 3 UNTRANSLATED REGION | HYDROPEROXIDE GLUTATHIONE-PEROXIDASE | Selenocysteine - metabolism | Codon, Terminator - genetics | Selenium - pharmacology | Liver - metabolism | Protein Biosynthesis - physiology | RNA, Transfer, Amino Acid-Specific - genetics | RNA, Transfer, Amino Acid-Specific - metabolism | Male | Mice, Transgenic | Codon, Terminator - metabolism | Animals | Selenocysteine - genetics | Protein Biosynthesis - drug effects | Mice | Dietary Supplements | Selenoproteins - biosynthesis | Selenoprotein | Protein Synthesis and Degradation | Selenocysteine | Transfer RNA (tRNA) | Selenium | Translation Control | Ribosome Profiling | Recoding
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9. Full Text Site-specific pK a determination of selenocysteine residues in selenovasopressin by using 77Se NMR spectroscopy
by Mobli, Mehdi and Morgenstern, David and King, Glenn F and Alewood, Paul F and Muttenthaler, Markus
Angewandte Chemie - International Edition, ISSN 1433-7851, 12/2011, Volume 50, Issue 50, pp. 11952 - 11955
selenocysteine | selective alkylation | selenovasopressin | NMR spectroscopy | values | Nuclear Magnetic Resonance, Biomolecular - methods | Selenocysteine - chemical synthesis | Humans | Selenocysteine - chemistry | Vasopressins - chemistry | Kinetics | Selenocysteine - analogs & derivatives
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10. Full Text SECISearch3 and Seblastian: New tools for prediction of SECIS elements and selenoproteins
by Mariotti, Marco and Lobanov, Alexei V and Guigo, Roderic and Gladyshev, Vadim N
Nucleic Acids Research, ISSN 0305-1048, 08/2013, Volume 41, Issue 15, pp. e149 - e149
Selenoproteins are proteins containing an uncommon amino acid selenocysteine (Sec). Sec is inserted by a specific translational machinery that recognizes a... 
IN-SILICO IDENTIFICATION | SELENOCYSTEINE INSERTION SYSTEM | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | GENES | AUREOCOCCUS-ANOPHAGEFFERENS | EUKARYOTES | GENERATION | ALIGNMENTS | GENOME | Amino Acid Sequence | Computational Biology - methods | Reproducibility of Results | Bacteria - chemistry | Selenoproteins - genetics | Humans | Selenocysteine - chemistry | Eukaryota - chemistry | Molecular Sequence Data | Bacteria - genetics | Selenoproteins - analysis | Selenoproteins - chemistry | Animals | Eukaryota - genetics | Selenocysteine - analysis | Selenocysteine - genetics | Software | Internet | Culture Media - chemistry | Nucleic Acid Conformation | Inverted Repeat Sequences | Evolution, Molecular | Selenoproteïnes | Compostos organoselènics | Biologia computacional | Methods Online
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11. Full Text Custom selenoprotein production enabled by laboratory evolution of recoded bacterial strains
by Thyer, Ross and Shroff, Raghav and Klein, Dustin R and D'Oelsnitz, Simon and Cotham, Victoria C and Byrom, Michelle and Brodbelt, Jennifer S and Ellington, Andrew D
Nature Biotechnology, ISSN 1087-0156, 08/2018, Volume 36, Issue 7, pp. 624 - 631
Incorporation of the rare amino acid selenocysteine to form diselenide bonds can improve stability and function of synthetic peptide therapeutics. However,... 
ORGANISMS | DISULFIDE-CONTAINING PROTEINS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SELENOCYSTEINE INSERTION | AMINO-ACIDS | GLUTATHIONE-PEROXIDASE | IN-VIVO | TRANSFER-RNA | TRANSLATION | ESCHERICHIA-COLI STRAIN | EXPRESSION | beta-Lactamases - genetics | Selenocysteine - genetics | Selenoproteins - genetics | Disulfides - chemistry | Escherichia coli - genetics | Selenocysteine - chemistry | Directed Molecular Evolution | Gene Expression Regulation, Bacterial | Selenoproteins - biosynthesis | Physiological aspects | Bacteria | Biosynthesis | Selenoproteins | Production processes | Methods | Incorporation | Disulfide bonds | Biological evolution | Fluorescence | Selenocysteine | Amino acids | Decoding | Proteins | Genetic code | E coli | Dependence | Evolution | Codons | Bonding | Strains (organisms) | Recombinant | Fitness
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12. Full Text Selective selenol fluorescent probes: Design, synthesis, structural determinants, and biological applications
by Zhang, Baoxin and Ge, Chunpo and Yao, Juan and Liu, Yaping and Xie, Huichen and Fang, Jianguo
Journal of the American Chemical Society, ISSN 0002-7863, 01/2015, Volume 137, Issue 2, pp. 757 - 769
Selenium (Se) is an essential micronutrient element, and the biological significance of Se is predominantly dependent on its incorporation as selenocysteine... 
OXIDATIVE STRESS | IN-VIVO | THIOPHENOLS | REACTIVITY | HL-60 CELLS | SELENOCYSTEINE | MEDIATED APOPTOSIS | GLUTATHIONE PEROXIDASE | CHEMISTRY, MULTIDISCIPLINARY | MAMMALIAN THIOREDOXIN REDUCTASE | LIVING CELLS | Fluorescent Dyes - chemical synthesis | Fluorescent Dyes - chemistry | Selenocysteine - metabolism | Chemistry Techniques, Synthetic | Cell Survival | Humans | Selenocysteine - chemistry | Substrate Specificity | Molecular Imaging | Selenium Compounds - chemical synthesis | Hep G2 Cells | Drug Design | Selenium Compounds - chemistry | HeLa Cells | Thioredoxin-Disulfide Reductase - chemistry | Protein biosynthesis | Hydrogen-ion concentration | Aqueous solution reactions | Analysis | Green fluorescent protein
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13. Full Text How selenium has altered our understanding of the genetic code
by Hatfield, Dolph L and Gladyshev, Vadim N
Molecular and Cellular Biology, ISSN 0270-7306, 2002, Volume 22, Issue 11, pp. 3565 - 3576
RAT-LIVER | DIETARY SELENIUM | ACTIVE-SITE | SELENOCYSTEINE TRANSFER-RNA | NONSENSE-MEDIATED DECAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | SERINE TRANSFER-RNA | FUNCTIONAL-CHARACTERIZATION | SELENOPROTEIN MESSENGER-RNAS | HYDROPEROXIDE GLUTATHIONE-PEROXIDASE | MAMMALIAN THIOREDOXIN REDUCTASE | CELL BIOLOGY | Selenium - chemistry | Selenocysteine - metabolism | Gene Expression | Genetic Code | Humans | RNA, Transfer, Amino Acyl - chemistry | Selenocysteine - chemistry | Molecular Sequence Data | RNA, Transfer, Amino Acyl - genetics | Proteins - genetics | Animals | Proteins - metabolism | Selenium - metabolism | Selenocysteine - genetics | Base Sequence | Codon - genetics | Proteins - chemistry | Selenoproteins | Nucleic Acid Conformation | Evolution, Molecular | Minireview
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14. Full Text Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities
by Lubos, Edith and Loscalzo, Joseph and Handy, Diane E
Antioxidants & Redox Signaling, ISSN 1523-0864, 10/2011, Volume 15, Issue 7, pp. 1957 - 1997
Reactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these... 
Comprehensive Invited Review | ISCHEMIA-REPERFUSION INJURY | GPX1 PRO198LEU POLYMORPHISM | ENDOTHELIAL PROGENITOR CELLS | SELENOCYSTEINE INSERTION-SEQUENCE | BREAST-CANCER RISK | MANGANESE SUPEROXIDE-DISMUTASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOCRINOLOGY & METABOLISM | MESSENGER-RNA STABILITY | NF-KAPPA-B | E-DEFICIENT MICE | CORONARY-ARTERY-DISEASE | Selenocysteine - metabolism | Neoplasms - etiology | Reactive Oxygen Species - metabolism | Oxidative Stress | Diabetes Mellitus - genetics | Glutathione Peroxidase - antagonists & inhibitors | Humans | Cardiovascular Diseases - therapy | Molecular Sequence Data | Cardiovascular Diseases - genetics | Neoplasms - therapy | Glutathione Peroxidase - chemistry | Neoplasms - genetics | Cell Death | Diabetes Mellitus - etiology | Amino Acid Sequence | Cardiovascular Diseases - etiology | Glutathione Peroxidase - metabolism | Gene Expression | Genetic Predisposition to Disease | Oxidation-Reduction | Risk Factors | Selenocysteine - chemistry | Enzyme Inhibitors - pharmacology | Gene Expression Regulation | Enzyme Inhibitors - therapeutic use | Glutathione Peroxidase - genetics | Polymorphism, Genetic | Animals | Diabetes Mellitus - therapy | Protein Conformation | Antioxidants | Active oxygen | Physiological aspects | Cellular signal transduction | Peroxidase | Research | Health aspects
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