Page last updated: 2024-08-17

nadp and selenocysteine

nadp has been researched along with selenocysteine in 21 studies

Research

Studies (21)

TimeframeStudies, this research(%)All Research%
pre-19901 (4.76)18.7374
1990's5 (23.81)18.2507
2000's9 (42.86)29.6817
2010's5 (23.81)24.3611
2020's1 (4.76)2.80

Authors

AuthorsStudies
Mizutani, T1
Björnstedt, M; Hamberg, M; Holmgren, A; Kumar, S; Xue, J1
Flohé, L; Marcocci, L; Packer, L1
Arnér, ES; Aslund, F; Holmgren, A; Ljung, J; Zhong, L1
Gorlatov, SN; Stadtman, TC1
Arnér, ES; Holmgren, A; Zhong, L1
Bar-Noy, S; Gorlatov, SN; Stadtman, TC1
Holmgren, A; Lindqvist, Y; Sandalova, T; Schneider, G; Zhong, L1
Holmgren, A; Zhong, L1
Guo, X; Jin, X; Qi, Y; Wang, M1
Diekert, G; Schmitz, RP1
del Arenal, IP; Guevara-Flores, A; Mendoza-Hernández, G; Plancarte, A; Rendón, JL; Uribe, A1
Damdimopoulos, AE; Nalvarte, I; Spyrou, G1
Cho, SH; Choi, CY; Kim, BH; Kim, JH; Kim, JR; Kim, YD; Kwon, J; Lee, SM; Lee, SR1
Fang, J; Holmgren, A; Lu, J1
Arnér, ES; Carvalho, CM; Holmgren, A; Lu, J; Zhang, X1
Board, PG; Fan, Z; Fang, J; Han, X; Liu, H; Lu, Z; Wei, J; Yin, L; Zhang, Y1
Cunniff, B; Fredette, N; Heintz, NH; Hondal, RJ; Snider, GW1
Dustin, CM; Hondal, RJ; Ruggles, EL; Snider, GW1
Arnér, ESJ; Benhar, M; Engelman, R; Ziv, T1
Bjørklund, G; Chasapis, CT; Peana, M; Wang, J; Zou, L1

Reviews

1 review(s) available for nadp and selenocysteine

ArticleYear
Thioredoxin reductase as a pharmacological target.
    Pharmacological research, 2021, Volume: 174

    Topics: Amino Acid Sequence; Animals; Antioxidants; Biomarkers; Enzyme Inhibitors; Genome-Wide Association Study; Humans; NADP; Oxidation-Reduction; Oxidative Stress; Protein Binding; Selenocysteine; Thioredoxin-Disulfide Reductase; Thioredoxins

2021

Other Studies

20 other study(ies) available for nadp and selenocysteine

ArticleYear
Some evidence of the enzymatic conversion of bovine suppressor phosphoseryl-tRNA to selenocysteyl-tRNA.
    FEBS letters, 1989, Jul-03, Volume: 250, Issue:2

    Topics: Amino Acids; Animals; Cattle; Chromatography, Thin Layer; Cysteine; Glutathione; NADP; RNA, Transfer; RNA, Transfer, Amino Acyl; Selenium; Selenocysteine; Transferases

1989
Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols.
    The Journal of biological chemistry, 1995, May-19, Volume: 270, Issue:20

    Topics: Catalysis; Cystine; Glutathione; Glutathione Transferase; Humans; Hydrogen Peroxide; Hydroxyeicosatetraenoic Acids; Leukotrienes; Lipid Peroxidation; Lipid Peroxides; MAP Kinase Kinase 1; Mitogen-Activated Protein Kinase Kinases; Models, Biological; NADP; Organoselenium Compounds; Oxidation-Reduction; Peroxides; Placenta; Protein Serine-Threonine Kinases; Protein-Tyrosine Kinases; Selenocysteine; tert-Butylhydroperoxide; Thioredoxin-Disulfide Reductase; Thioredoxins

1995
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
Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue.
    The Journal of biological chemistry, 1998, Apr-10, Volume: 273, Issue:15

    Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Catalysis; Cattle; Cloning, Molecular; Consensus Sequence; Conserved Sequence; DNA, Complementary; Glutathione Reductase; Humans; Liver; Models, Molecular; Molecular Sequence Data; NADP; Nucleic Acid Conformation; Peptide Fragments; Pyridines; Rats; Selenium; Selenocysteine; Sequence Alignment; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Thioredoxin-Disulfide Reductase; Thymus Gland

1998
Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin.
    Proceedings of the National Academy of Sciences of the United States of America, 1998, Jul-21, Volume: 95, Issue:15

    Topics: Alkylation; Amino Acid Sequence; Catalysis; Chromatography, High Pressure Liquid; HeLa Cells; Heparin; Humans; NADP; Oxidation-Reduction; Selenocysteine; Thioredoxin-Disulfide Reductase

1998
Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence.
    Proceedings of the National Academy of Sciences of the United States of America, 2000, May-23, Volume: 97, Issue:11

    Topics: Animals; Binding Sites; Cattle; Cysteine; Glutathione Reductase; Mass Spectrometry; Models, Molecular; NADP; Oxidation-Reduction; Selenocysteine; Thioredoxin-Disulfide Reductase

2000
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
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
Mammalian thioredoxin reductases as hydroperoxide reductases.
    Methods in enzymology, 2002, Volume: 347

    Topics: Animals; Cattle; Electron Transport; Female; Humans; Hydrogen Peroxide; Methods; Mice; Models, Biological; NADP; Oxidation-Reduction; Pregnancy; Rats; Selenocysteine; Thioredoxin-Disulfide Reductase

2002
[Light-dependent incorporation of selenite into selenocysteine by isolated chromatophore of Chromatium vinosum].
    Wei sheng wu xue bao = Acta microbiologica Sinica, 1999, Volume: 39, Issue:3

    Topics: Catalysis; Chromatium; Glutathione; Glutathione Reductase; Light; NADP; Selenocysteine; Serine; Sodium Selenite

1999
Purification and properties of the formate dehydrogenase and characterization of the fdhA gene of Sulfurospirillum multivorans.
    Archives of microbiology, 2003, Volume: 180, Issue:6

    Topics: Amino Acid Sequence; Chromatography; DNA, Bacterial; Enzyme Stability; Epsilonproteobacteria; Escherichia coli Proteins; Formate Dehydrogenases; Formates; Guanine Nucleotides; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Membrane Transport Proteins; Molecular Sequence Data; Molecular Weight; NAD; NADP; Paraquat; Protein Sorting Signals; Protein Subunits; Pterins; Selenocysteine; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Temperature

2003
Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci).
    Molecular and biochemical parasitology, 2004, Volume: 133, Issue:1

    Topics: Amino Acid Sequence; Ammonium Sulfate; Animals; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange; Cysticercus; Dimerization; Fractional Precipitation; Glutathione; Isoelectric Point; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes; NADH, NADPH Oxidoreductases; NADP; Protein Subunits; Selenocysteine; Sequence Analysis, Protein; Substrate Specificity; Taenia; Thioredoxins

2004
Human mitochondrial thioredoxin reductase reduces cytochrome c and confers resistance to complex III inhibition.
    Free radical biology & medicine, 2004, May-15, Volume: 36, Issue:10

    Topics: Anti-Bacterial Agents; Antifungal Agents; Antimycin A; Cell Division; Cell Survival; Cells, Cultured; Cytochromes c; Electron Transport; Electron Transport Complex III; Humans; Kidney; Methacrylates; Mitochondria; NAD; NADP; Selenocysteine; Thiazoles; Thioredoxin Reductase 1; Thioredoxin Reductase 2; Thioredoxin-Disulfide Reductase; Thioredoxins

2004
Oxidation of thioredoxin reductase in HeLa cells stimulated with tumor necrosis factor-alpha.
    FEBS letters, 2004, Jun-04, Volume: 567, Issue:2-3

    Topics: Animals; Apoptosis; Cysteine; Cytoplasm; Disulfides; DNA Fragmentation; Genes, Dominant; HeLa Cells; Humans; Hydrogen Peroxide; Mitochondria, Liver; Mutation; NADP; Oxidation-Reduction; Rats; Recombinant Proteins; Selenocysteine; Thioredoxin Reductase 1; Thioredoxin Reductase 2; Thioredoxin-Disulfide Reductase; Tumor Necrosis Factor-alpha

2004
Thioredoxin reductase is irreversibly modified by curcumin: a novel molecular mechanism for its anticancer activity.
    The Journal of biological chemistry, 2005, Jul-01, Volume: 280, Issue:26

    Topics: Animals; Anions; Antineoplastic Agents; Binding Sites; Cell Nucleus; Curcuma; Curcumin; Cysteine; Cytosol; Dose-Response Relationship, Drug; HeLa Cells; Humans; Inhibitory Concentration 50; Mass Spectrometry; Mitochondria; Models, Biological; Models, Chemical; NADP; NADPH Oxidases; Oxidants; Oxidation-Reduction; Peptides; Plant Extracts; Protein Binding; Rats; Selenocysteine; Superoxides; Temperature; Thioredoxin-Disulfide Reductase; Time Factors

2005
Effects of selenite and chelating agents on mammalian thioredoxin reductase inhibited by mercury: implications for treatment of mercury poisoning.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011, Volume: 25, Issue:1

    Topics: Animals; Biocatalysis; Catalytic Domain; Cell Survival; Chelating Agents; Cysteine; Dose-Response Relationship, Drug; Enzyme Activation; Glutathione; HEK293 Cells; Humans; Mercuric Chloride; Mercury; Mercury Compounds; Mercury Poisoning; Methylmercury Compounds; Molecular Structure; NADP; Rats; Recombinant Proteins; Selenium Compounds; Selenocysteine; Sodium Selenite; Spectrometry, Mass, Electrospray Ionization; Thioredoxin-Disulfide Reductase

2011
Expression of selenocysteine-containing glutathione S-transferase in eukaryote.
    Protein expression and purification, 2012, Volume: 84, Issue:1

    Topics: Blotting, Western; Cloning, Molecular; Codon; Genetic Vectors; Glutathione Transferase; HEK293 Cells; Humans; NADP; Recombinant Proteins; Selenocysteine

2012
A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates.
    Analytical biochemistry, 2013, Dec-01, Volume: 443, Issue:1

    Topics: Animals; Cell Line; Cystine; Enzyme Assays; Epithelial Cells; Mice; NADP; Organoselenium Compounds; Oxidation-Reduction; Respiratory Mucosa; Selenocysteine; Sensitivity and Specificity; Spectrophotometry; Thioredoxin-Disulfide Reductase

2013
A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum.
    Biochemistry, 2014, Jan-28, Volume: 53, Issue:3

    Topics: Amino Acid Sequence; Catalysis; Cystine; Kinetics; Models, Chemical; NADP; Organoselenium Compounds; Oxidation-Reduction; Plasmodium falciparum; Selenocysteine; Substrate Specificity; Thioredoxin-Disulfide Reductase

2014
Inhibitory nitrosylation of mammalian thioredoxin reductase 1: Molecular characterization and evidence for its functional role in cellular nitroso-redox imbalance.
    Free radical biology & medicine, 2016, Volume: 97

    Topics: Amino Acid Sequence; Animals; Catalytic Domain; Cysteine; Glutathione; HeLa Cells; Humans; NADP; Nitric Oxide Donors; Oxidation-Reduction; Protein Processing, Post-Translational; Rats; S-Nitrosothiols; Selenocysteine; Thioredoxin Reductase 1

2016