selenocysteine and dithionitrobenzoic acid

selenocysteine has been researched along with dithionitrobenzoic acid in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (42.86)18.2507
2000's4 (57.14)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Liu, SY; Stadtman, TC1
Flohé, L; Marcocci, L; Packer, L1
Baines, IC; Kang, SW; Rhee, SG1
Bar-Noy, S; Gorlatov, SN; Stadtman, TC1
Gromer, S; Gross, JH1
Eckenroth, BE; Everse, SJ; Hondal, RJ; Rould, MA1
Eckenroth, BE; Flemer, S; Hondal, RJ; Lacey, BM1

Other Studies

7 other study(ies) available for selenocysteine and dithionitrobenzoic acid

ArticleYear
Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells.
    Proceedings of the National Academy of Sciences of the United States of America, 1997, Jun-10, Volume: 94, Issue:12

    Topics: Adenocarcinoma; Amino Acid Sequence; Base Sequence; Binding Sites; Chromatography, Affinity; Chromatography, Gel; Chromatography, High Pressure Liquid; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; HeLa Cells; Heparin; Humans; Kinetics; Lung Neoplasms; Peptide Fragments; Placenta; Selenium; Selenocysteine; Thioredoxin-Disulfide Reductase; Tumor Cells, Cultured

1997
Evidence for a functional relevance of the selenocysteine residue in mammalian thioredoxin reductase.
    BioFactors (Oxford, England), 1997, Volume: 6, Issue:3

    Topics: Animals; Cattle; Cell Line; Culture Media; Dithionitrobenzoic Acid; Glutathione Reductase; Humans; NADP; Selenocysteine; Sodium Selenite; Structure-Activity Relationship; Thioredoxin-Disulfide Reductase

1997
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
Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity.
    Free radical biology & medicine, 2001, Jan-01, Volume: 30, Issue:1

    Topics: Animals; Catalysis; Chemical Phenomena; Chemistry, Physical; Chromatography, High Pressure Liquid; Codon; Dimerization; Dithionitrobenzoic Acid; Escherichia coli; Flavin-Adenine Dinucleotide; Formate Dehydrogenases; Gene Expression; Humans; Hydrogenase; Kinetics; Multienzyme Complexes; Mutation; NADP; Rats; Recombinant Proteins; Selenium; Selenocysteine; Solubility; Structure-Activity Relationship; Substrate Specificity; Thioredoxin-Disulfide Reductase

2001
Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium.
    The Journal of biological chemistry, 2002, Mar-22, Volume: 277, Issue:12

    Topics: Animals; Antineoplastic Agents; Catalysis; Dithionitrobenzoic Acid; Drosophila melanogaster; Glutathione Disulfide; Glutathione Reductase; Humans; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Mice; Models, Biological; Models, Chemical; Organoselenium Compounds; Peroxidase; Placenta; Plasmodium falciparum; Protein Binding; Protein Structure, Tertiary; Selenium; Selenocysteine; Silver; Substrate Specificity; Thioredoxin-Disulfide Reductase; Thioredoxins; Time Factors

2002
Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases.
    Biochemistry, 2007, Apr-24, Volume: 46, Issue:16

    Topics: Amino Acid Sequence; Animals; Catalysis; Crystallization; Crystallography, X-Ray; Cysteine; Dithionitrobenzoic Acid; Drosophila melanogaster; Mice; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides; Selenocysteine; Thioredoxin-Disulfide Reductase

2007
Selenium in thioredoxin reductase: a mechanistic perspective.
    Biochemistry, 2008, Dec-02, Volume: 47, Issue:48

    Topics: Animals; Dithionitrobenzoic Acid; Drosophila melanogaster; Hydrogen-Ion Concentration; Oxidation-Reduction; Peptides, Cyclic; Selenium; Selenocysteine; Spectrum Analysis; Sulfides; Thioredoxin-Disulfide Reductase

2008