Compounds > selenocysteine

selenocysteine and dithiothreitol

selenocysteine has been researched along with dithiothreitol in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19902 (20.00)18.7374
1990's1 (10.00)18.2507
2000's7 (70.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Esaki, N; Karai, N; Soda, K; Tanaka, H1
Burnell, JN; Karle, JA; Shrift, A1
Baines, IC; Kang, SW; Rhee, SG1
Chen, M; Ding, L; Lian, G; Liu, L; Ni, J; Zhao, D1
Lacourciere, G; Ogasawara, Y; Stadtman, TC1
Klootwijk, W; Kuiper, GG; Visser, TJ1
Darras, VM; Flik, G; Haasdijk, R; Klaren, PH; Metz, JR; Nitsch, LM; Van der Geyten, S1
Gladyshev, VN; Kim, HY1
Kim, HY; Lee, TH1
Hondal, RJ; Lothrop, AP; Ruggles, EL1

Other Studies

10 other study(ies) available for selenocysteine and dithiothreitol

ArticleYear
Reaction and regulation mechanisms of selenocysteine beta-lyase.
    Progress in clinical and biological research, 1984, Volume: 144A

    Topics: Aluminum; Animals; Cysteine; Dithiothreitol; Keto Acids; Liver; Lyases; Magnetic Resonance Spectroscopy; Pyridoxal Phosphate; Pyridoxamine; Selenium; Selenocysteine; Swine

1984
Reduction of DL-selenocystine and isolation of L-seleoncysteine.
    Journal of inorganic biochemistry, 1980, Volume: 12, Issue:4

    Topics: Amino Acyl-tRNA Synthetases; Borohydrides; Chemistry, Organic; Cysteine; Cystine; Dithiothreitol; Mercaptoethanol; Methods; Organic Chemistry Phenomena; Organoselenium Compounds; Oxidation-Reduction; Paracoccus denitrificans; Plants; Selenium; Selenocysteine; Substrate Specificity

1980
Characterization of a mammalian peroxiredoxin that contains one conserved cysteine.
    The Journal of biological chemistry, 1998, Mar-13, Volume: 273, Issue:11

    Topics: Amino Acid Sequence; Conserved Sequence; Cysteine; Disulfides; Dithionitrobenzoic Acid; Dithiothreitol; Glutathione Peroxidase; Humans; Hydrogen Peroxide; Models, Chemical; Molecular Sequence Data; Neoplasm Proteins; Oxidation-Reduction; Peroxidases; Peroxiredoxin III; Peroxiredoxins; Phospholipases A; Phospholipases A2; Proteins; Recombinant Proteins; Selenocysteine; Sequence Homology, Amino Acid; Subcellular Fractions

1998
A selenium-containing catalytic antibody with Type I deiodinase activity.
    Biochemical and biophysical research communications, 2001, May-25, Volume: 283, Issue:5

    Topics: Amino Acid Substitution; Animals; Antibodies, Catalytic; Antibodies, Monoclonal; Dithiothreitol; Haptens; Iodide Peroxidase; Kinetics; Mice; Mice, Inbred BALB C; Propylthiouracil; Selenocysteine; Serine; Thyroxine

2001
Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Aug-14, Volume: 98, Issue:17

    Topics: Animals; Cattle; Dithiothreitol; Glutathione; Iodoacetamide; Oxidation-Reduction; Phosphates; Selenium; Selenium Compounds; Selenocysteine; Sodium Selenite; Thiosulfate Sulfurtransferase

2001
Substitution of cysteine for a conserved alanine residue in the catalytic center of type II iodothyronine deiodinase alters interaction with reducing cofactor.
    Endocrinology, 2002, Volume: 143, Issue:4

    Topics: Alanine; Amino Acid Substitution; Animals; Catalysis; COS Cells; Cysteine; Dithiothreitol; Genetic Vectors; Humans; Iodide Peroxidase; Iodothyronine Deiodinase Type II; Kinetics; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Selenocysteine; Thyroxine; Triiodothyronine

2002
Characterization of an iodothyronine 5'-deiodinase in gilthead seabream (Sparus auratus) that is inhibited by dithiothreitol.
    Endocrinology, 2005, Volume: 146, Issue:12

    Topics: Amino Acid Sequence; Animals; Base Sequence; Codon; Consensus Sequence; Dithiothreitol; DNA, Complementary; Iodide Peroxidase; Iodine; Kidney; Kinetics; Microsomes; Molecular Sequence Data; Open Reading Frames; Sea Bream; Selenocysteine; Triiodothyronine, Reverse

2005
Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases.
    PLoS biology, 2005, Volume: 3, Issue:12

    Topics: Amino Acid Sequence; Animals; Binding Sites; Catalysis; Conserved Sequence; Cysteine; Dithiothreitol; Evolution, Molecular; Humans; Kinetics; Methionine Sulfoxide Reductases; Molecular Sequence Data; Mutation; Oxidoreductases; Selenocysteine; Sequence Alignment; Thioredoxins

2005
An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide.
    Archives of biochemistry and biophysics, 2008, Oct-15, Volume: 478, Issue:2

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Catalytic Domain; Cell Line; Clostridium; Cysteine; Dithiothreitol; DNA Primers; Humans; Kinetics; Methionine; Methionine Sulfoxide Reductases; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Recombinant Proteins; Selenocysteine; Sequence Homology, Amino Acid; Thioredoxins

2008
No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue.
    Biochemistry, 2009, Jul-07, Volume: 48, Issue:26

    Topics: Amino Acid Substitution; Animals; Auranofin; Aurothioglucose; Biocatalysis; Caenorhabditis elegans; Cystine; Dinitrobenzenes; Dithiothreitol; Drosophila melanogaster; Enzyme Inhibitors; Gene Deletion; Glutathione; Hydrogen-Ion Concentration; Kinetics; Mice; Models, Chemical; Organoselenium Compounds; Recombinant Proteins; Selenium; Selenocysteine; Sodium Selenite; Substrate Specificity; Thioctic Acid; Thioredoxin Reductase 2; Thioredoxin-Disulfide Reductase

2009