3-acetylpyridine adenine dinucleotide has been researched along with nadp in 29 studies
Studies (3-acetylpyridine adenine dinucleotide) | Trials (3-acetylpyridine adenine dinucleotide) | Recent Studies (post-2010) (3-acetylpyridine adenine dinucleotide) | Studies (nadp) | Trials (nadp) | Recent Studies (post-2010) (nadp) |
---|---|---|---|---|---|
68 | 0 | 2 | 21,608 | 25 | 3,484 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 7 (24.14) | 18.7374 |
1990's | 19 (65.52) | 18.2507 |
2000's | 3 (10.34) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cleland, WW; Cook, PF; Gavva, SR; Harris, BG; Urbauer, JL; Weiss, PM | 1 |
Morrison, JF; Stone, SR | 1 |
Bragg, PD; Clarke, DM | 1 |
Hatefi, Y; Phelps, DC | 1 |
Garel, JR; Müller, K | 1 |
Fisher, RR; Pennington, RM | 1 |
Chen, S; Guillory, RJ; Jeng, SJ | 1 |
Bragg, PD; Glavas, NA | 1 |
Hatefi, Y; Yamaguchi, M | 2 |
Bizouarn, T; Cotton, NP; Grimley, RL; Hutton, M; Jackson, JB; Stilwell, SN | 1 |
Hu, X; Persson, A; Rydström, J; Zhang, JW | 1 |
Bizouarn, T; Day, JM; Hutton, M; Jackson, JB | 1 |
Cook, PF; Karsten, WE | 1 |
Bizouarn, T; Jackson, JB | 1 |
Bhatnagar, A; Liu, SQ; Srivastava, SK | 1 |
Cotton, NP; Jackson, JB; Palmer, T; Thomas, CM; Williams, R | 1 |
Kasper, CB; Shen, AL | 1 |
Bizouarn, T; Cotton, NP; Diggle, C; Jackson, JB | 1 |
Bragg, PD | 1 |
Bizouarn, T; Diggle, C; Grimley, R; Jackson, JB; Thomas, CM | 1 |
Bizouarn, T; Cotton, NP; Jackson, JB; Stilwell, S; Venning, J | 1 |
Bragg, PD; Hou, C | 1 |
Bradshaw, DE; Cleland, WW; Urbauer, JL | 1 |
Claiborne, A; Mallett, TC; Parsonage, D | 1 |
Axelsson, M; Bizouarn, T; Egorov, MV; Fjellström, O; Ivanova, MV; Korneenko, TV; Pestov, NB; Rydström, J; Shakhparonov, M | 1 |
Imai, T | 1 |
BRUNNEMANN, A; COPER, H | 1 |
Hirst, J; Yakovlev, G | 1 |
29 other study(ies) available for 3-acetylpyridine adenine dinucleotide and nadp
Article | Year |
---|---|
Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.
Topics: Animals; Ascaris; Carbon Isotopes; Chickens; Decarboxylation; Deuterium; Kinetics; Liver; Malate Dehydrogenase; Malates; NAD; NADP; Oxidation-Reduction; Substrate Specificity | 1991 |
Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates.
Topics: Deuterium; Escherichia coli; Folic Acid; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; Tetrahydrofolate Dehydrogenase; Viscosity | 1988 |
Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli.
Topics: Allosteric Site; Catalysis; Cytoplasm; Dicyclohexylcarbodiimide; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Oxidation-Reduction; Peptide Fragments; Solubility; Spectrometry, Fluorescence | 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.
Topics: Animals; Binding Sites; Carbodiimides; Dicyclohexylcarbodiimide; In Vitro Techniques; Mitochondria; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Protons; Quinolines | 1984 |
The interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH.
Topics: Aspartokinase Homoserine Dehydrogenase; Binding Sites; Escherichia coli; Kinetics; Multienzyme Complexes; NAD; NADP; Oxidation-Reduction; Protein Binding | 1984 |
Reconstituted mitochondrial transhydrogenase is a transmembrane protein.
Topics: Animals; Cattle; Liposomes; Mitochondria, Heart; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Photic Stimulation; Taurine | 1983 |
Current applications of the photoaffinity technique to the study of the structure of complex I.
Topics: Affinity Labels; Alcohol Oxidoreductases; Animals; Azides; beta-Alanine; Cattle; Magnetic Resonance Spectroscopy; NAD; NAD(P)H Dehydrogenase (Quinone); NADH, NADPH Oxidoreductases; NADP; Photochemistry; Pyrimidine Nucleotides; Quinone Reductases; Ubiquinone | 1980 |
The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Escherichia coli; Hydrogen; Hydrogen-Ion Concentration; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Trypsin | 1995 |
Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction.
Topics: Amino Acid Sequence; Escherichia coli; Molecular Sequence Data; Mutation; NAD; NADP; NADP Transhydrogenases; Structure-Activity Relationship | 1995 |
The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli.
Topics: Escherichia coli; Kinetics; NAD; NADP; NADP Transhydrogenases | 1995 |
Characterization of the interaction of NADH with proton pumping E. coli transhydrogenase reconstituted in the absence and in the presence of bacteriorhodopsin.
Topics: Bacteriorhodopsins; Binding Sites; Escherichia coli; Histidine; NAD; NADP; NADP Transhydrogenases | 1995 |
Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with analogues of the nucleotide substrates.
Topics: Binding Sites; Dicyclohexylcarbodiimide; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protons; Solubility | 1994 |
Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.
Topics: Animals; Ascaris; Carboxylic Acids; Catalysis; Chickens; Horses; Isotopes; Malate Dehydrogenase; NAD; NADP; Oxaloacetates; Oxidation-Reduction | 1994 |
The ratio of protons translocated/hydride ion equivalent transferred by nicotinamide nucleotide transhydrogenase in chromatophores from Rhodospirillum rubrum.
Topics: Bacterial Chromatophores; Coenzymes; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protons; Rhodospirillum rubrum; Spectrophotometry, Ultraviolet | 1993 |
Bovine lens aldose reductase. pH-dependence of steady-state kinetic parameters and nucleotide binding.
Topics: Aldehyde Reductase; Animals; Cattle; Coenzymes; Hydrogen-Ion Concentration; Kinetics; Lens, Crystalline; Mathematics; Models, Theoretical; NAD; NADP; Oxidation-Reduction; Protein Binding; Substrate Specificity | 1993 |
Inhibition of proton-translocating transhydrogenase from photosynthetic bacteria by N,N'-dicyclohexylcarbodiimide.
Topics: Amino Acid Sequence; Binding Sites; Dicyclohexylcarbodiimide; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Peptide Fragments; Rhodobacter capsulatus; Rhodospirillum rubrum | 1993 |
Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential.
Topics: Base Sequence; Cytochrome c Group; Dithionite; DNA Primers; Electron Transport; Ferricyanides; Flavin-Adenine Dinucleotide; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Polymerase Chain Reaction; Serine; Spectrophotometry | 1996 |
Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum.
Topics: Binding Sites; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Kinetics; Models, Chemical; NAD; NADP; NADP Transhydrogenases; Nucleotides; Protein Binding; Recombinant Proteins; Rhodospirillum rubrum; Spectrometry, Fluorescence; Spectrophotometry | 1996 |
Mechanism of hydride transfer during the reduction of 3-acetylpyridine adenine dinucleotide by NADH catalyzed by the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Binding Sites; Escherichia coli; Kinetics; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protons | 1996 |
High cyclic transhydrogenase activity catalyzed by expressed and reconstituted nucleotide-binding domains of Rhodospirillum rubrum transhydrogenase.
Topics: Animals; Base Sequence; Binding Sites; Cattle; DNA Primers; Escherichia coli; In Vitro Techniques; Kinetics; Molecular Structure; Molecular Weight; NAD; NADP; NADP Transhydrogenases; Protein Conformation; Recombinant Proteins; Rhodospirillum rubrum | 1997 |
Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer.
Topics: Hydrogen; Mutation; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Rhodospirillum rubrum; Tyrosine | 1997 |
The pH dependences of reactions catalyzed by the complete proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains.
Topics: Bacterial Chromatophores; Binding Sites; Electron Transport; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; NADP Transhydrogenases; Protons; Recombinant Proteins; Rhodospirillum rubrum | 1997 |
Effect of truncation and mutation of the carboxyl-terminal region of the beta subunit on membrane assembly and activity of the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Cell Membrane; Escherichia coli; Kinetics; Molecular Sequence Data; Mutation; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Conformation; Sequence Deletion | 1998 |
Determination of the kinetic and chemical mechanism of malic enzyme using (2R,3R)-erythro-fluoromalate as a slow alternate substrate.
Topics: Animals; Carbon Isotopes; Catalysis; Cattle; Chickens; Coenzymes; Decarboxylation; Deuterium; Kinetics; Malate Dehydrogenase; Malates; NAD; NADP; Oxaloacetates; Rabbits; Substrate Specificity; Swine | 1998 |
Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center.
Topics: Bacterial Proteins; Binding Sites; Coenzymes; Cysteine; Dithionite; Electron Transport; Enzyme Stability; Hydrogen-Ion Concentration; Multienzyme Complexes; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; NADP; Oxidation-Reduction; Recombinant Proteins; Serine; Spectrometry, Fluorescence; Sulfenic Acids | 1999 |
Interactions between the soluble domain I of nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and transhydrogenase from Escherichia coli. Effects on catalytic and H+-pumping activities.
Topics: Amino Acid Sequence; Animals; Antibodies, Bacterial; Antibodies, Monoclonal; Bacterial Proteins; Catalysis; Detergents; Escherichia coli; Hydrogen-Ion Concentration; Liposomes; Mice; Mice, Inbred BALB C; Models, Molecular; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Protein Binding; Protein Conformation; Protein Denaturation; Protein Multimerization; Protein Structure, Tertiary; Protons; Recombinant Fusion Proteins; Rhodospirillum rubrum; Trypsin | 2000 |
Substrate specificity of mammalian pyridine nucleotide transglycosidases.
Topics: Animals; Cattle; Glycoside Hydrolases; Guinea Pigs; Hydrolysis; Kinetics; Liver; Multienzyme Complexes; N-Glycosyl Hydrolases; NAD; NADP; Niacin; Nicotinamide Mononucleotide; Rabbits; Spectrophotometry; Spleen; Substrate Specificity; Swine; Transferases | 2002 |
[HYDROLYSIS OF NAD(P) AND BIOSYNTHESIS OF 3-APAD(P) BY BRAIN MICROSOMES OF DIFFERENT ANIMAL SPECIES].
Topics: Animals; Brain; Hydrolysis; Microsomes; NAD; NADP; Nucleotides; Research | 1965 |
Transhydrogenation reactions catalyzed by mitochondrial NADH-ubiquinone oxidoreductase (Complex I).
Topics: Animals; Cattle; Electron Transport Complex I; Hydrogen; Mitochondria, Heart; NAD; NADP | 2007 |