nad has been researched along with 2,6-dichloroindophenol in 34 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 19 (55.88) | 18.7374 |
| 1990's | 7 (20.59) | 18.2507 |
| 2000's | 5 (14.71) | 29.6817 |
| 2010's | 3 (8.82) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Gan, EV; Haberman, HF; Menon, IA | 1 |
| Dancey, GF; Shapiro, BM | 1 |
| Fujii, K; Galivan, JH; Huennekens, FM | 1 |
| Barton, LL; Deyhle, RR | 1 |
| Gatt, S; Hollander, PM | 1 |
| Hochstein, LI | 1 |
| Bartfai, T; Gatt, S; Hollander, PM | 1 |
| Horiike, K; Miyake, Y; Nakamura, Y; Takayama, N | 1 |
| Dooijewaard, G; Slater, EC | 2 |
| Gan, EV; Haberman, HF; Lam, KM; Menon, IA | 1 |
| de Vries, J; Nauta, WT; van Bree, L; Verboom, CN | 1 |
| Aogaichi, T; Beach, RL; Plaut, GW | 1 |
| Kamiński, ZW; Zakrzewska, B | 1 |
| Avraam, R; Kotliar, AB | 1 |
| Halsall, HB; Heineman, WR; Tang, HT | 1 |
| Hajizadeh, K; Halsall, HB; Heineman, WR; Tang, HT | 1 |
| Beattie, DS; Sprague, SG; Zhu, QS | 1 |
| Lingens, F; Markus, A; Ruf, HH; Schweizer, D; Seez, M | 1 |
| Akino, M; Hasegawa, H; Nakanishi, N; Yamada, S | 1 |
| Bannasch, P; Mayer, D; Naumann, R | 1 |
| Cornelisse, CJ; Schor, NA | 1 |
| Tsai, CS | 1 |
| Halsall, HB; Heineman, WR; Jenkins, SH; Yao, H | 1 |
| Bayer, M; Simon, H; Walter, K | 1 |
| Blasco, R; Castillo, F; Martínez-Luque, M | 1 |
| Jaiswal, AK | 1 |
| Boyd, C; Cousins, K; Daya, S; Heron, P | 1 |
| Pardo, JP; Velázquez, I | 1 |
| Alvarez-Tinaut, MC; Espinosa, F; Garrido, I | 1 |
| Brown, AM; Efimov, AV; Gazaryan, IG; Kazakov, SV; Klyachko, NL; Kristal, BS; Shchedrina, VA | 1 |
| Baumann, U; Mermod, M; Mourlane, F; Oberholzer, AE; Solioz, M; Waltersperger, S | 1 |
| Bilitewski, U; Hassan, RY | 1 |
| Abendroth, J; Begley, DW; Edwards, TE; Gardberg, AS; Haft, DH; Lorimer, DD; Marathias, VM; Mayclin, SJ; Myler, PJ; Phan, IQ; Pierce, PG; Staker, BL; Sullivan, A | 1 |
34 other study(ies) available for nad and 2,6-dichloroindophenol
| Article | Year |
|---|---|
Electron transfer properties of melanin.
Topics: 2,6-Dichloroindophenol; Cytochrome c Group; Electron Transport; Energy Transfer; Ferricyanides; Kinetics; Melanins; NAD; NADP; Oxidation-Reduction | 1976 |
The NADH dehydrogenase of the respiratory chain of Escherichia coli. II. Kinetics of the purified enzyme and the effects of antibodies elicited against it on membrane-bound and free enzyme.
Topics: 2,6-Dichloroindophenol; Antibodies; Cell Membrane; Escherichia coli; Ferricyanides; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Immunodiffusion; Immunoelectrophoresis; Kinetics; NAD; NADH, NADPH Oxidoreductases; Oxygen Consumption; Vitamin K | 1976 |
Activation of methionine synthase: further characterization of flavoprotein system.
Topics: 2,6-Dichloroindophenol; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; Dithionite; Enzyme Activation; Escherichia coli; Ferricyanides; Flavin-Adenine Dinucleotide; Flavoproteins; Kinetics; Methyltransferases; NAD; NADP; Oxidation-Reduction; Paraquat; Vitamin K | 1977 |
Nicotinamide adenine dinucleotide -- independent formate dehydrogenase in Mycobacterium phlei.
Topics: 2,6-Dichloroindophenol; Aldehyde Oxidoreductases; Cell-Free System; Cytochrome c Group; Electron Transport; Formates; Hydrogen-Ion Concentration; Mycobacterium; Mycobacterium phlei; NAD; Oxidation-Reduction; Subcellular Fractions; Tetrazolium Salts | 1977 |
Studies on high molecular weight modifiers of the nonhyperbolic V versus (S) curves of DT-diaphorase.
Topics: 2,6-Dichloroindophenol; Animals; Kinetics; Liver; Lysophosphatidylcholines; Molecular Weight; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Polyethylene Glycols; Quaternary Ammonium Compounds; Quinone Reductases; Rats; Structure-Activity Relationship | 1975 |
Studies of a halophilic NADH dehydrogenase. II. Kinetic properties of the enzyme in relation to salt activation.
Topics: 2,6-Dichloroindophenol; Anions; Bacteria; Cations, Monovalent; Hot Temperature; Kinetics; NAD; NADH, NADPH Oxidoreductases; Sodium | 1975 |
Studies on the reaction mechanism of DT diaphorase. Intermediary plateau and trough regions in the initial velocity vs substrate concentration curves.
Topics: 2,6-Dichloroindophenol; Animals; Drug Stability; Kinetics; Liver; Mathematics; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Protein Binding; Protein Conformation; Quinone Reductases; Rats; Regression Analysis; Temperature; Time Factors | 1975 |
Alpha reduced nicotinamide adenine dinucleotide-dependent reductase reactions of rat liver microsomes.
Topics: 2,6-Dichloroindophenol; Adenosine Diphosphate; Animals; Cytochromes; Dose-Response Relationship, Drug; Kinetics; Male; Microsomes, Liver; NAD; NADH, NADPH Oxidoreductases; NADPH-Ferrihemoprotein Reductase; Rats; Stereoisomerism | 1975 |
Steady-state kinetics of high molecular weight (type-I) NADH dehydrogenase.
Topics: 2,6-Dichloroindophenol; Animals; Ferricyanides; Isoenzymes; Kinetics; Mathematics; Molecular Weight; Myocardium; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction | 1976 |
Steady-state kinetics of low molecular weight (type-II) NADH dehydrogenase.
Topics: 2,6-Dichloroindophenol; Cytochrome Reductases; Ferricyanides; Isoenzymes; Kinetics; Mathematics; Mitochondria; Molecular Weight; NAD; NADH, NADPH Oxidoreductases | 1976 |
Oxidizing and reducing properties of melanins.
Topics: 2,6-Dichloroindophenol; Ferricyanides; Melanins; NAD; Oxidation-Reduction | 1977 |
Reduction of 2,6-dichlorophenol indophenol by bovine methemoglobin reductase in the presence of a number of non-steroidal anti-inflammatory compounds.
Topics: 2,6-Dichloroindophenol; Animals; Anti-Inflammatory Agents; Cattle; Cytochrome-B(5) Reductase; Indophenol; Kinetics; NAD; NADH, NADPH Oxidoreductases; Phenindione; Phenylbutazone | 1977 |
Substrate activity of structural analogs of isocitrate for isocitrate dehydrogenases from bovine heart.
Topics: 2,6-Dichloroindophenol; Animals; Cattle; Chromatography, Paper; Chromatography, Thin Layer; Dinitrophenols; Isocitrate Dehydrogenase; Isocitrates; Kinetics; Lactones; Mitochondria, Muscle; Myocardium; NAD; NADP; Optical Rotation; Oxidation-Reduction; Pyruvaldehyde; Structure-Activity Relationship; Tricarboxylic Acids | 1975 |
Involvement of histidine residues in catalytic activity of xanthine dehydrogenase from hen liver.
Topics: 2,6-Dichloroindophenol; Animals; Chickens; Diethyl Pyrocarbonate; Enzyme Activation; Female; Histidine; Kinetics; Liver; NAD; Oxidation-Reduction; Photochemistry; Structure-Activity Relationship; Xanthine; Xanthine Dehydrogenase; Xanthines | 1992 |
[Inhibition of NADH-dehydrogenase by low concentrations of NAD+].
Topics: 2,6-Dichloroindophenol; Animals; Catalysis; Cattle; Kinetics; Mitochondria, Heart; NAD; NADH Dehydrogenase; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxygen | 1991 |
Electrochemical enzyme immunoassay for phenytoin by flow-injection analysis incorporating a redox coupling agent.
Topics: 2,6-Dichloroindophenol; Electrochemistry; Electrodes; Humans; Immunoenzyme Techniques; NAD; Oxidation-Reduction; Phenytoin | 1991 |
Flow-injection analysis with electrochemical detection of reduced nicotinamide adenine dinucleotide using 2,6-dichloroindophenol as a redox coupling agent.
Topics: 2,6-Dichloroindophenol; Carbon; Electrochemistry; Electrodes; Electron Transport; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Oxygen | 1991 |
Reduction of exogenous quinones and 2,6-dichlorophenol indophenol in cytochrome b-deficient yeast mitochondria: a differential effect on center i and center o of the cytochrome b-c1 complex.
Topics: 2,6-Dichloroindophenol; Antimycin A; Binding Sites; Chlorophyll; Cytochrome b Group; Electron Transport; Electron Transport Complex III; Indophenol; Light-Harvesting Protein Complexes; Methacrylates; Mitochondria; Mutation; NAD; Photosynthetic Reaction Center Complex Proteins; Plant Proteins; Quinones; Succinates; Succinic Acid; Thiazoles; Yeasts | 1988 |
Purification and some properties of component B of the 4-chlorophenylacetate 3,4-dioxygenase from Pseudomonas species strain CBS 3.
Topics: 2,6-Dichloroindophenol; Amino Acids; Cytochrome c Group; Dioxygenases; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Isoelectric Point; Kinetics; Macromolecular Substances; Molecular Weight; NAD; Oxygenases; Pseudomonas | 1987 |
Catalytic properties of NADPH-specific dihydropteridine reductase from bovine liver.
Topics: 2,6-Dichloroindophenol; Animals; Catalysis; Cattle; Dihydropteridine Reductase; Hydroxylation; Kinetics; Liver; NAD; NADH, NADPH Oxidoreductases; NADP; Phenylalanine; Thyroxine | 1986 |
Investigation of the carbohydrate metabolism of normal and neoplastic hepatocytes using 2,6-dichlorophenolindophenol as a probe for NAD(P)H production measured by voltammetry.
Topics: 2,6-Dichloroindophenol; Animals; Carbohydrate Metabolism; Cell Line; Coloring Agents; Electrochemistry; Glucose; Indophenol; Liver; Liver Neoplasms, Experimental; Male; NAD; NADP; Oxidation-Reduction; Oxygen; Potentiometry; Rats; Rats, Inbred Strains | 1985 |
Biochemical and quantitative histochemical study of reduced pyridine nucleotide dehydrogenation by human colonic carcinomas.
Topics: 2,6-Dichloroindophenol; Aged; Colonic Neoplasms; Cytochrome c Group; Cytochrome Reductases; Female; Humans; Intestinal Mucosa; Male; Middle Aged; NAD; NADH Dehydrogenase; NADH, NADPH Oxidoreductases; NADP; NADPH Dehydrogenase | 1983 |
Kinetic studies of multifunctional reactions catalysed by lipoamide dehydrogenase.
Topics: 2,6-Dichloroindophenol; Animals; Dihydrolipoamide Dehydrogenase; Ferricyanides; Kinetics; Mathematics; NAD; Swine; Thioctic Acid | 1980 |
Electrochemical dehydrogenase-based homogeneous assays in whole blood.
Topics: 2,6-Dichloroindophenol; Blood Glucose; Electrochemistry; Electrodes; Erythrocytes; Hematocrit; Hexokinase; Humans; Hydroxymercuribenzoates; Immunoenzyme Techniques; Indicators and Reagents; NAD; Oxidation-Reduction; Oxidoreductases; Quality Control; Sensitivity and Specificity; Theophylline | 1995 |
Purification and partial characterisation of a reversible artificial mediator accepting NADH oxidoreductase from Clostridium thermoaceticum.
Topics: 2,6-Dichloroindophenol; Amino Acid Sequence; Anthraquinones; Clostridium; Enzyme Stability; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Iron; Molecular Sequence Data; Molecular Weight; NAD; NADP Transhydrogenases; Paraquat; Sequence Analysis; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Sulfur | 1996 |
The assimilatory nitrate reductase from the phototrophic bacterium, Rhodobacter capsulatus E1F1, is a flavoprotein.
Topics: 2,6-Dichloroindophenol; Cytochrome c Group; Dihydrolipoamide Dehydrogenase; Dimerization; Electron Transport; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; Flavoproteins; Kinetics; Molecular Weight; NAD; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Protein Conformation; Rhodobacter capsulatus; Spectrophotometry | 1997 |
Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases.
Topics: 2,6-Dichloroindophenol; Animals; Cholic Acids; Chromatography, Ion Exchange; Cytosol; Detergents; Dicumarol; Enzyme Activation; Enzyme Inhibitors; Fractional Precipitation; Immune Sera; Isoenzymes; Microsomes, Liver; Molecular Weight; NAD; NAD(P)H Dehydrogenase (Quinone); NADP; p-Chloromercuribenzoic Acid; Rats; Rats, Inbred F344; Sulfhydryl Reagents; Vitamin K | 2000 |
Paradoxical effects of copper and manganese on brain mitochondrial function.
Topics: 2,6-Dichloroindophenol; Animals; Brain Chemistry; Coloring Agents; Copper; In Vitro Techniques; L-Lactate Dehydrogenase; Lactic Acid; Malates; Male; Manganese; Mitochondria; Monoamine Oxidase; NAD; Oxidation-Reduction; Rats; Rats, Wistar; Succinic Acid | 2001 |
Kinetic characterization of the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae.
Topics: 2,6-Dichloroindophenol; Adenosine Monophosphate; Binding, Competitive; Dose-Response Relationship, Drug; Electron Transport Complex I; Enzyme Activation; Enzyme Stability; Flavin-Adenine Dinucleotide; Flavones; Flavonoids; Hydrogen-Ion Concentration; Mitochondria; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Quinones; Rotenone; Saccharomyces cerevisiae | 2001 |
Effect of dichlorophenolindophenol, dichlorophenolindophenol-sulfonate, and cytochrome c on redox capacity and simultaneous net H+/K+ fluxes in aeroponically grown seedling roots of sunflower (Helianthus annuus L.): new evidence for a plasma membrane CN(-
Topics: 2,6-Dichloroindophenol; Cell Membrane; Cyanides; Cytochrome c Group; Helianthus; Hydrogen-Ion Concentration; Models, Biological; NAD; Oxidation-Reduction; Plant Roots; Potassium; Protons; Sulfonic Acids | 2001 |
pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification.
Topics: 2,6-Dichloroindophenol; Animals; Chromatography, Gel; Dihydrolipoamide Dehydrogenase; Hydrogen-Ion Concentration; Kinetics; Micelles; Myocardium; NAD; Protein Structure, Quaternary; Protein Structure, Tertiary; Substrate Specificity; Swine | 2005 |
Structure and function of CinD (YtjD) of Lactococcus lactis, a copper-induced nitroreductase involved in defense against oxidative stress.
Topics: 2,6-Dichloroindophenol; 4-Nitroquinoline-1-oxide; Bacterial Proteins; Cadmium; Catalase; Copper; Crystallography, X-Ray; Flavoproteins; Gene Deletion; Gene Expression Profiling; Kinetics; Lactococcus lactis; Models, Molecular; Molecular Sequence Data; NAD; Nitroreductases; Oxidants; Oxidation-Reduction; Oxidative Stress; Protein Structure, Tertiary; Reverse Transcriptase Polymerase Chain Reaction; Silver; Stress, Physiological | 2010 |
A viability assay for Candida albicans based on the electron transfer mediator 2,6-dichlorophenolindophenol.
Topics: 2,6-Dichloroindophenol; Candida albicans; Candida glabrata; Catalysis; Color; Electrochemistry; Electron Transport; Enzyme Activation; Fungal Proteins; Galactose; Glucose; Microbial Viability; Microbiological Techniques; NAD; NADH Dehydrogenase; Oxidation-Reduction; Oxygen; Rotenone; Saccharomyces cerevisiae; Spectrophotometry | 2011 |
Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.
Topics: 2,6-Dichloroindophenol; Binding Sites; Coenzymes; Crystallography, X-Ray; Cyclohexane Monoterpenes; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Monoterpenes; Mutagenesis, Insertional; Mycobacterium tuberculosis; NAD; Oxidoreductases; Protein Binding; Protein Conformation; Thiazoles | 2017 |