Page last updated: 2024-08-17

nad and dihydrolipoamide

nad has been researched along with dihydrolipoamide in 14 studies

Research

Studies (14)

TimeframeStudies, this research(%)All Research%
pre-19906 (42.86)18.7374
1990's4 (28.57)18.2507
2000's1 (7.14)29.6817
2010's2 (14.29)24.3611
2020's1 (7.14)2.80

Authors

AuthorsStudies
Blanchard, JS; Leichus, BN1
Sahlman, L; Williams, CH1
Rahmatullah, M; Roche, TE1
Hummel, BC; Sawada, K; Walfish, PG1
Goswami, A; Rosenberg, IN1
Tsai, CS1
Becker, DM; Kark, RA; Knipprath, WG; Nissenson, C; Perlman, SL1
Liu, TC; Patel, MS; Vettakkorumakankav, NN1
Guest, JR; Maeda-Yorita, K; Massey, V; Russell, GC; Williams, CH1
Fischer, GM; Gallyas, F; Kispal, G; Sumegi, B; Szabados, E1
Forster, MJ; Prokai, L; Shu, H; Yan, LJ; Yang, SH1
Fukamichi, T; Nishimoto, E1
Krishnan, C; Sarangi, A1
Chandra, P; Chiranjivi, AK; Dubey, VK; Prakash, J; Saha, G1

Other Studies

14 other study(ies) available for nad and dihydrolipoamide

ArticleYear
Pig heart lipoamide dehydrogenase: solvent equilibrium and kinetic isotope effects.
    Biochemistry, 1992, Mar-31, Volume: 31, Issue:12

    Topics: Animals; Catalysis; Dihydrolipoamide Dehydrogenase; Disulfides; Dithiothreitol; Hydrogen-Ion Concentration; Kinetics; Myocardium; NAD; Solvents; Substrate Specificity; Swine; Thioctic Acid

1992
Lipoamide dehydrogenase from Escherichia coli. Steady-state kinetics of the physiological reaction.
    The Journal of biological chemistry, 1989, May-15, Volume: 264, Issue:14

    Topics: Animals; Dihydrolipoamide Dehydrogenase; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Myocardium; NAD; Oxidation-Reduction; Phosphorylation; Spectrophotometry; Swine; Thioctic Acid

1989
Component requirements for NADH inhibition and spermine stimulation of pyruvate dehydrogenaseb phosphatase activity.
    The Journal of biological chemistry, 1988, Jun-15, Volume: 263, Issue:17

    Topics: Alkylation; Animals; Calcium; Cattle; Enzyme Activation; Ethylmaleimide; NAD; Phosphoprotein Phosphatases; Pyruvate Dehydrogenase (Lipoamide)-Phosphatase; Spermine; Thioctic Acid

1988
Cytosolic cofactors and dihydrolipoamide stimulate hepatic microsomal 5'-deiodination.
    Endocrinology, 1985, Volume: 117, Issue:3

    Topics: Animals; Cytosol; Dihydrolipoamide Dehydrogenase; Dithiothreitol; Iodide Peroxidase; Male; Microsomes, Liver; NAD; Peroxidases; Rats; Rats, Inbred Strains; Thioctic Acid

1985
Stimulation of iodothyronine outer ring monodeiodinase by dihydrolipoamide.
    Endocrinology, 1983, Volume: 112, Issue:4

    Topics: Animals; Dicumarol; Dithiothreitol; Enzyme Activation; Iodide Peroxidase; Kidney; Kinetics; Microsomes; NAD; Peroxidases; Propylthiouracil; Rats; Temperature; Thioctic Acid

1983
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
Optimal conditions for the assay of lipoamide dehydrogenase in homogenized human platelets.
    Clinica chimica acta; international journal of clinical chemistry, 1982, May-06, Volume: 121, Issue:1

    Topics: Blood Platelets; Dihydrolipoamide Dehydrogenase; Humans; Hydrogen-Ion Concentration; Kinetics; Methods; NAD; Thioctic Acid

1982
Dihydrolipoamide dehydrogenase: activity assays.
    Methods in enzymology, 1995, Volume: 252

    Topics: Animals; Dihydrolipoamide Dehydrogenase; Eukaryotic Cells; Humans; NAD; Oxidation-Reduction; Prokaryotic Cells; Rats; Species Specificity; Swine; Thioctic Acid

1995
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
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
Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE.
    Electrophoresis, 2007, Volume: 28, Issue:7

    Topics: Animals; Chromatography, Liquid; Dihydrolipoamide Dehydrogenase; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Ethylmaleimide; Mitochondrial Proteins; NAD; Nitroblue Tetrazolium; Oxidation-Reduction; Rats; Rats, Sprague-Dawley; Spectrometry, Mass, Electrospray Ionization; Staining and Labeling; Tandem Mass Spectrometry; Thioctic Acid

2007
Conformational Change Near the Redox Center of Dihydrolipoamide Dehydrogenase Induced by NAD(+) to Regulate the Enzyme Activity.
    Journal of fluorescence, 2015, Volume: 25, Issue:3

    Topics: Catalysis; Catalytic Domain; Dihydrolipoamide Dehydrogenase; Electron Transport; Flavin-Adenine Dinucleotide; NAD; Oxidation-Reduction; Protein Conformation; Thioctic Acid

2015
Detoxification of hexavalent chromium by Leucobacter sp. uses a reductase with specificity for dihydrolipoamide.
    Journal of basic microbiology, 2016, Volume: 56, Issue:2

    Topics: Actinobacteria; Biotransformation; Chromatography, Liquid; Chromium; Coenzymes; Dihydrolipoamide Dehydrogenase; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Hydrogen-Ion Concentration; Mass Spectrometry; Molecular Weight; NAD; NADP; Oxidoreductases; Spectrophotometry; Temperature; Thioctic Acid

2016
Mutational studies on Leishmania donovani dihydrolipoamide dehydrogenase (LdBPK291950.1) indicates that the enzyme may not be classical class-I pyridine nucleotide-disulfide oxidoreductase.
    International journal of biological macromolecules, 2020, Dec-01, Volume: 164

    Topics: Amino Acid Sequence; Amino Acid Substitution; Catalysis; Catalytic Domain; Dihydrolipoamide Dehydrogenase; Disulfides; Leishmania donovani; Mutation; NAD; Nucleotides; Oxidoreductases; Pyridines; Sequence Alignment; Thioctic Acid

2020