Compounds > eedq
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eedq and nad

eedq has been researched along with nad in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's2 (40.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hatefi, Y; Phelps, DC2
Hatefi, Y; Yamaguchi, M1
Belogrudov, G; Hatefi, Y1
Berrisford, JM; Sazanov, LA; Thompson, CJ1

Other Studies

5 other study(ies) available for eedq and nad

ArticleYear
Mitochondrial nicotinamide nucleotide transhydrogenase: nonidentical modification by N,N'-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline at the NAD(H) binding site.
    Archives of biochemistry and biophysics, 1985, Nov-15, Volume: 243, Issue:1

    Topics: Adenosine Monophosphate; Animals; Binding Sites; Carbodiimides; Cattle; Dicyclohexylcarbodiimide; Kinetics; Mitochondria, Heart; NAD; NADH, NADPH Oxidoreductases; NADP Transhydrogenases; Quinolines; Sepharose

1985
Effects of N,N'-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline on hydride ion transfer and proton translocation activities of mitochondrial nicotinamidenucleotide transhydrogenase.
    Biochemistry, 1984, Dec-18, Volume: 23, Issue:26

    Topics: Animals; Binding Sites; Carbodiimides; Dicyclohexylcarbodiimide; In Vitro Techniques; Mitochondria; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Protons; Quinolines

1984
Energy-transducing nicotinamide nucleotide transhydrogenase. Nucleotide binding properties of the purified enzyme and proteolytic fragments.
    The Journal of biological chemistry, 1993, Aug-25, Volume: 268, Issue:24

    Topics: Amino Acid Sequence; Aniline Compounds; Animals; Binding Sites; Carbon Radioisotopes; Cattle; Dicyclohexylcarbodiimide; Glutamates; Glutamic Acid; Kinetics; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Peptide Fragments; Quinolines

1993
Catalytic sector of complex I (NADH:ubiquinone oxidoreductase): subunit stoichiometry and substrate-induced conformation changes.
    Biochemistry, 1994, Apr-19, Volume: 33, Issue:15

    Topics: Binding Sites; Catalysis; Cross-Linking Reagents; Energy Transfer; Ferricyanides; Immunoblotting; Iron-Sulfur Proteins; Molecular Weight; NAD; NAD(P)H Dehydrogenase (Quinone); NADP; Neurospora crassa; Protein Conformation; Quinolines

1994
Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus.
    Biochemistry, 2008, Sep-30, Volume: 47, Issue:39

    Topics: Bacterial Proteins; Dithionite; Dithiothreitol; Electron Transport Complex I; Escherichia coli; Escherichia coli Proteins; NAD; Protein Subunits; Quinolines; Reactive Oxygen Species; Thermus thermophilus

2008