Page last updated: 2024-08-17

nad and lipoamide

nad has been researched along with lipoamide in 11 studies

Research

Studies (11)

TimeframeStudies, this research(%)All Research%
pre-19904 (36.36)18.7374
1990's3 (27.27)18.2507
2000's3 (27.27)29.6817
2010's1 (9.09)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Richarme, G1
Huang, RR; Spector, A; Wang, RR; Yan, GZ1
Cronshaw, AD; Jocelyn, PC1
Tsai, CS1
Guest, JR; Maeda-Yorita, K; Massey, V; Russell, GC; Williams, CH1
Hol, WG; Kalk, KH; Mattevi, A; Obmolova, G; van Berkel, WJ1
Fischer, GM; Gallyas, F; Kispal, G; Sumegi, B; Szabados, E1
Bryk, R; Erdjument-Bromage, H; Lima, CD; Nathan, C; Tempst, P1
Argyrou, A; Blanchard, JS; Palfey, BA1
Argyrou, A; Blanchard, JS; Palfey, BA; Sun, G1
Arango, N; Bryk, R; Lima, CD; Nathan, C; Park, YH; Patel, MS; Venugopal, A; Warren, JD1

Other Studies

11 other study(ies) available for nad and lipoamide

ArticleYear
[Reconstitution of high-affinity galactose transport of Salmonella typhimurium in proteoliposomes: energization by lipoamide and NAD or by the membrane potential; inhibition by ATP].
    Comptes rendus de l'Academie des sciences. Serie III, Sciences de la vie, 1987, Volume: 305, Issue:3

    Topics: Adenosine Triphosphate; Calcium-Binding Proteins; Carrier Proteins; Cell Membrane; Galactose; Kinetics; Liposomes; Membrane Potentials; Monosaccharide Transport Proteins; NAD; Periplasmic Binding Proteins; Proteolipids; Salmonella typhimurium; Thioctic Acid

1987
Thioredoxin fragment 31-36 is reduced by dihydrolipoamide and reduces oxidized protein.
    Biochemical and biophysical research communications, 1988, Jan-15, Volume: 150, Issue:1

    Topics: Bacterial Proteins; Crystallins; Dihydrolipoamide Dehydrogenase; Disulfides; Escherichia coli; Glyceraldehyde-3-Phosphate Dehydrogenases; Insulin; Kinetics; NAD; Oxidation-Reduction; Peptide Fragments; Proteins; Spectrophotometry; Thioctic Acid; Thioredoxin-Disulfide Reductase; Thioredoxins

1988
The reduction of disulphides by rat liver mitochondria.
    Biochimica et biophysica acta, 1984, Feb-14, Volume: 797, Issue:2

    Topics: Animals; Disulfides; Glutathione; Kinetics; Mitochondria, Liver; NAD; NADP; Oxidation-Reduction; Rats; Structure-Activity Relationship; Sulfhydryl Compounds; Thioctic Acid

1984
Kinetic studies of multifunctional reactions catalysed by lipoamide dehydrogenase.
    The International journal of biochemistry, 1980, Volume: 11, Issue:5

    Topics: 2,6-Dichloroindophenol; Animals; Dihydrolipoamide Dehydrogenase; Ferricyanides; Kinetics; Mathematics; NAD; Swine; Thioctic Acid

1980
Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R.
    Biochemistry, 1994, May-24, Volume: 33, Issue:20

    Topics: Circular Dichroism; Dihydrolipoamide Dehydrogenase; Electrochemistry; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Lysine; NAD; Oxidation-Reduction; Photochemistry; Spectrometry, Fluorescence; Spectrophotometry; Thioctic Acid

1994
Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties.
    Journal of molecular biology, 1993, Apr-20, Volume: 230, Issue:4

    Topics: Amino Acid Sequence; Azotobacter vinelandii; Binding Sites; Catalysis; Crystallization; Dihydrolipoamide Dehydrogenase; Electronic Data Processing; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Mutation; NAD; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Pseudomonas fluorescens; Recombinant Proteins; Sequence Homology, Amino Acid; Thioctic Acid; X-Ray Diffraction

1993
Enhanced ADP-ribosylation and its diminution by lipoamide after ischemia-reperfusion in perfused rat heart.
    Free radical biology & medicine, 1999, Volume: 27, Issue:9-10

    Topics: Adenosine Diphosphate Ribose; ADP Ribose Transferases; Animals; Antioxidants; DNA Damage; Enzyme Activation; In Vitro Techniques; Lipid Peroxidation; Male; Mitochondria, Heart; Myocardial Reperfusion Injury; NAD; Perfusion; Poly(ADP-ribose) Polymerases; Proteins; Rats; Rats, Wistar; Reactive Oxygen Species; Thioctic Acid

1999
Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein.
    Science (New York, N.Y.), 2002, Feb-08, Volume: 295, Issue:5557

    Topics: Acyltransferases; Amino Acid Sequence; Antioxidants; Binding Sites; Catalysis; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Dihydrolipoamide Dehydrogenase; Hydrogen Bonding; Hydrogen Peroxide; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; NAD; Oxidation-Reduction; Oxidoreductases; Peroxidases; Peroxiredoxins; Peroxynitrous Acid; Protein Conformation; Protein Folding; Protein Structure, Quaternary; Thioctic Acid; Thioredoxins

2002
The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis.
    Biochemistry, 2002, Dec-10, Volume: 41, Issue:49

    Topics: Bacterial Proteins; Catalysis; Dihydrolipoamide Dehydrogenase; Electron Transport; Flavin-Adenine Dinucleotide; Models, Chemical; Mycobacterium tuberculosis; NAD; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Thermodynamics; Thioctic Acid

2002
Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level.
    Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

    Topics: Bacterial Proteins; Benzoquinones; Catalysis; Dihydrolipoamide Dehydrogenase; Flavin-Adenine Dinucleotide; Kinetics; Mycobacterium tuberculosis; NAD; Oxidants; Oxidation-Reduction; Oxygen; Pentanoic Acids; Recombinant Proteins; Spectrophotometry; Substrate Specificity; Thioctic Acid

2003
Triazaspirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase .
    Biochemistry, 2010, Mar-02, Volume: 49, Issue:8

    Topics: Animals; Antitubercular Agents; Binding Sites; Cell Survival; Cells, Cultured; Crystallography, X-Ray; Dihydrolipoamide Dehydrogenase; Enzyme Inhibitors; Macrophages; Mice; Models, Biological; Molecular Structure; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; NAD; Structure-Activity Relationship; Thioctic Acid

2010