glutathione disulfide has been researched along with flavin-adenine dinucleotide in 8 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (12.50) | 18.7374 |
1990's | 3 (37.50) | 18.2507 |
2000's | 4 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Asencio, C; Kaakoush, NO; Mégraud, F; Mendz, GL | 1 |
Losada, M; Rivas, J; Serrano, A | 1 |
Becker, K; Bergmann, B; Müller, S; Schirmer, RH; Walter, RD | 1 |
Davies, JE; delCardayre, SB; Fahey, RC; Newton, GL; Stock, KP | 1 |
Danielson, UH; Hansson, LO; Jiang, F; Mannervik, B | 1 |
Csermely, P; Jakus, J; Korcsmáros, T; Nardai, G; Papp, E; Stadler, K | 1 |
Desbois, A; Picaud, T | 1 |
Li, D; Lin, T; Qu, JY; Yang, MS; Zheng, JJ; Zheng, W | 1 |
8 other study(ies) available for glutathione disulfide and flavin-adenine dinucleotide
Article | Year |
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A redox basis for metronidazole resistance in Helicobacter pylori.
Topics: Anti-Infective Agents; Bacterial Proteins; Drug Resistance, Bacterial; Electrophoresis, Gel, Two-Dimensional; FMN Reductase; Gene Expression Profiling; Gene Expression Regulation, Bacterial; Helicobacter Infections; Helicobacter pylori; Humans; Mass Spectrometry; Metronidazole; Microbial Sensitivity Tests; Mutation; Nitroreductases; Oxidation-Reduction; Proteome | 2009 |
Purification and properties of glutathione reductase from the cyanobacterium Anabaena sp. strain 7119.
Topics: Amino Acids; Cyanobacteria; Flavin-Adenine Dinucleotide; Glutathione; Glutathione Disulfide; Glutathione Reductase; Hydrogen-Ion Concentration; Isoelectric Point; Kinetics; Molecular Weight; NADP; Oxidation-Reduction; Substrate Specificity; Sulfhydryl Reagents; Zinc | 1984 |
Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-binding sites.
Topics: Amino Acid Sequence; Animals; Binding Sites; DNA Primers; DNA, Protozoan; Flavin-Adenine Dinucleotide; Genes, Protozoan; Glutathione; Glutathione Disulfide; Glutathione Reductase; Humans; Models, Molecular; Molecular Sequence Data; Molecular Structure; NADP; Plasmodium falciparum; Polymerase Chain Reaction; Sequence Homology, Amino Acid | 1995 |
Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme.
Topics: Bacterial Proteins; Binding Sites; Coenzyme A; Flavin-Adenine Dinucleotide; Flavoproteins; Glutathione Disulfide; Kinetics; Molecular Conformation; Molecular Structure; NADH, NADPH Oxidoreductases; NADP; Oxidation-Reduction; Staphylococcus aureus; Sulfhydryl Compounds | 1998 |
Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site.
Topics: Amino Acid Sequence; Anabaena; Binding Sites; Catalysis; Flavin-Adenine Dinucleotide; Glutathione Disulfide; Glutathione Reductase; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP; Recombinant Proteins; Sepharose; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity | 1999 |
Diabetic changes in the redox status of the microsomal protein folding machinery.
Topics: Animals; Ascorbic Acid; Dehydroascorbic Acid; Diabetes Mellitus, Experimental; Flavin-Adenine Dinucleotide; Glutathione Disulfide; Male; Microsomes, Liver; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Protein Disulfide-Isomerases; Protein Folding; Rats; Rats, Wistar | 2005 |
Interaction of glutathione reductase with heavy metal: the binding of Hg(II) or Cd(II) to the reduced enzyme affects both the redox dithiol pair and the flavin.
Topics: Binding Sites; Cadmium; Flavin-Adenine Dinucleotide; Flavins; Glutathione Disulfide; Glutathione Reductase; Mercury; Oxidation-Reduction; Protein Binding; Reactive Oxygen Species; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Static Electricity | 2006 |
Increase in intracellular free/bound NAD[P]H as a cause of Cd-induced oxidative stress in the HepG(2) cells.
Topics: Binding Sites; Cadmium Chloride; Cell Line, Tumor; Flavin-Adenine Dinucleotide; Glutathione; Glutathione Disulfide; Humans; NADP; Oxidative Stress; Protein Binding; Reactive Oxygen Species; Spectrometry, Fluorescence; Time Factors | 2008 |