nad has been researched along with lipoamide in 11 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 4 (36.36) | 18.7374 |
1990's | 3 (27.27) | 18.2507 |
2000's | 3 (27.27) | 29.6817 |
2010's | 1 (9.09) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Richarme, G | 1 |
Huang, RR; Spector, A; Wang, RR; Yan, GZ | 1 |
Cronshaw, AD; Jocelyn, PC | 1 |
Tsai, CS | 1 |
Guest, JR; Maeda-Yorita, K; Massey, V; Russell, GC; Williams, CH | 1 |
Hol, WG; Kalk, KH; Mattevi, A; Obmolova, G; van Berkel, WJ | 1 |
Fischer, GM; Gallyas, F; Kispal, G; Sumegi, B; Szabados, E | 1 |
Bryk, R; Erdjument-Bromage, H; Lima, CD; Nathan, C; Tempst, P | 1 |
Argyrou, A; Blanchard, JS; Palfey, BA | 1 |
Argyrou, A; Blanchard, JS; Palfey, BA; Sun, G | 1 |
Arango, N; Bryk, R; Lima, CD; Nathan, C; Park, YH; Patel, MS; Venugopal, A; Warren, JD | 1 |
11 other study(ies) available for nad and lipoamide
Article | Year |
---|---|
[Reconstitution of high-affinity galactose transport of Salmonella typhimurium in proteoliposomes: energization by lipoamide and NAD or by the membrane potential; inhibition by ATP].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 .
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 |