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glutathione disulfide and flavin-adenine dinucleotide

glutathione disulfide has been researched along with flavin-adenine dinucleotide in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19901 (12.50)18.7374
1990's3 (37.50)18.2507
2000's4 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Asencio, C; Kaakoush, NO; Mégraud, F; Mendz, GL1
Losada, M; Rivas, J; Serrano, A1
Becker, K; Bergmann, B; Müller, S; Schirmer, RH; Walter, RD1
Davies, JE; delCardayre, SB; Fahey, RC; Newton, GL; Stock, KP1
Danielson, UH; Hansson, LO; Jiang, F; Mannervik, B1
Csermely, P; Jakus, J; Korcsmáros, T; Nardai, G; Papp, E; Stadler, K1
Desbois, A; Picaud, T1
Li, D; Lin, T; Qu, JY; Yang, MS; Zheng, JJ; Zheng, W1

Other Studies

8 other study(ies) available for glutathione disulfide and flavin-adenine dinucleotide

ArticleYear
A redox basis for metronidazole resistance in Helicobacter pylori.
    Antimicrobial agents and chemotherapy, 2009, Volume: 53, Issue:5

    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.
    Journal of bacteriology, 1984, Volume: 158, Issue:1

    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.
    Molecular and biochemical parasitology, 1995, Volume: 74, Issue:1

    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.
    The Journal of biological chemistry, 1998, Mar-06, Volume: 273, Issue:10

    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.
    Biochemistry, 1999, Jul-20, Volume: 38, Issue:29

    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.
    Biochemical and biophysical research communications, 2005, Sep-02, Volume: 334, Issue:3

    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.
    Biochemistry, 2006, Dec-26, Volume: 45, Issue:51

    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.
    Toxicology, 2008, May-02, Volume: 247, Issue:1

    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