selenocysteine and flavin-adenine dinucleotide

selenocysteine has been researched along with flavin-adenine dinucleotide in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (16.67)18.2507
2000's4 (66.67)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Liu, SY; Stadtman, TC1
Bar-Noy, S; Gorlatov, SN; Stadtman, TC1
Fujii, J; Fujii, T; Fujiwara, N; Taniguchi, N1
Holmgren, A; Lindqvist, Y; Sandalova, T; Schneider, G; Zhong, L1
Björnstedt, M; Nordman, T; Olsson, JM1
Capacho, AS; Machuqueiro, M; Teixeira, VH1

Reviews

1 review(s) available for selenocysteine and flavin-adenine dinucleotide

ArticleYear
Extramitochondrial reduction of ubiquinone by flavoenzymes.
    Methods in enzymology, 2004, Volume: 378

    Topics: Animals; Antioxidants; Cytosol; Dihydrolipoamide Dehydrogenase; Dimerization; Disulfides; Escherichia coli; Flavin-Adenine Dinucleotide; Glutathione Reductase; Humans; Hydrogen-Ion Concentration; Kinetics; NAD(P)H Dehydrogenase (Quinone); Oxidation-Reduction; Selenocysteine; Structure-Activity Relationship; Substrate Specificity; Thioredoxin-Disulfide Reductase; Ubiquinone

2004

Other Studies

5 other study(ies) available for selenocysteine and flavin-adenine dinucleotide

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
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
Roles of N-terminal active cysteines and C-terminal cysteine-selenocysteine in the catalytic mechanism of mammalian thioredoxin reductase.
    Journal of biochemistry, 2001, Volume: 129, Issue:5

    Topics: Animals; Baculoviridae; Catalysis; COS Cells; Cysteine; Electron Transport; Flavin-Adenine Dinucleotide; Insecta; Mammals; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Tertiary; Rats; Selenocysteine; Thioredoxin-Disulfide Reductase; Thioredoxins

2001
Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Aug-14, Volume: 98, Issue:17

    Topics: Amino Acid Sequence; Animals; Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Evolution, Molecular; Flavin-Adenine Dinucleotide; Glutathione Reductase; Hydrogen Bonding; Mammals; Models, Molecular; Molecular Sequence Data; NADP; Oxidation-Reduction; Prokaryotic Cells; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rats; Selenocysteine; Sequence Homology, Amino Acid; Species Specificity; Thioredoxin-Disulfide Reductase

2001
The role of electrostatics in TrxR electron transfer mechanism: A computational approach.
    Proteins, 2016, Volume: 84, Issue:12

    Topics: Amino Acid Motifs; Coenzymes; Cysteine; Electron Transport; Electrons; Flavin-Adenine Dinucleotide; Humans; Hydrogen-Ion Concentration; Molecular Dynamics Simulation; Monte Carlo Method; Mutation; Oxidation-Reduction; Poisson Distribution; Protein Domains; Protein Structure, Secondary; Selenocysteine; Static Electricity; Thioredoxin Reductase 1; Water

2016