selenocysteine has been researched along with dithionitrobenzoic acid in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (42.86) | 18.2507 |
2000's | 4 (57.14) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Liu, SY; Stadtman, TC | 1 |
Flohé, L; Marcocci, L; Packer, L | 1 |
Baines, IC; Kang, SW; Rhee, SG | 1 |
Bar-Noy, S; Gorlatov, SN; Stadtman, TC | 1 |
Gromer, S; Gross, JH | 1 |
Eckenroth, BE; Everse, SJ; Hondal, RJ; Rould, MA | 1 |
Eckenroth, BE; Flemer, S; Hondal, RJ; Lacey, BM | 1 |
7 other study(ies) available for selenocysteine and dithionitrobenzoic acid
Article | Year |
---|---|
Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells.
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.
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.
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.
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.
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.
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.
Topics: Animals; Dithionitrobenzoic Acid; Drosophila melanogaster; Hydrogen-Ion Concentration; Oxidation-Reduction; Peptides, Cyclic; Selenium; Selenocysteine; Spectrum Analysis; Sulfides; Thioredoxin-Disulfide Reductase | 2008 |