nad has been researched along with glyceraldehyde 3-phosphate in 36 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 11 (30.56) | 18.7374 |
| 1990's | 10 (27.78) | 18.2507 |
| 2000's | 8 (22.22) | 29.6817 |
| 2010's | 6 (16.67) | 24.3611 |
| 2020's | 1 (2.78) | 2.80 |
| Authors | Studies |
|---|---|
| Huskey, WP; Liu, L | 1 |
| Batke, J; Vas, M | 1 |
| Cane, DE; Sohng, JK | 1 |
| Asryants, RA; Douzhenkova, IV; Nagradova, NK | 1 |
| Kvassman, J; Pettersson, G; Ryde-Pettersson, U | 1 |
| Orosz, F; Ovádi, J | 1 |
| Casazza, JP; Veech, RL | 1 |
| Aithal, HN; Toback, FG; Walsh-Reitz, MM | 1 |
| Kálmán, M; Nuridsány, M; Ovádi, J | 1 |
| Bland, J; Davison, AJ; Kong, S | 1 |
| Buttery, JE; Chamberlain, BR; Milner, CR | 1 |
| Copeland, L; Zammit, A | 1 |
| Kayastha, AM; Malhotra, OP; Tikoo, K | 1 |
| Dukes, ID; McIntyre, MS; Mertz, RJ; Philipson, LH; Roe, MW; Spencer, B; Worley, JF | 1 |
| Asryants, RA; Kuzminskaya, EV; Nagradova, NK | 1 |
| Bulargina, TV; Sergienko, EA; Severin, ES | 1 |
| Iwami, Y; Schachtele, CF; Yamada, T | 1 |
| Boschi-Muller, S; Branlant, G | 1 |
| De Graaf, AA; Moritz, B; Sahm, H; Striegel, K | 1 |
| Kim, JY; Park, CG; Park, HW; Yun, M | 1 |
| Jones, AR; Piccolo, F | 1 |
| Cleaves, HJ; Miller, SL | 1 |
| Jonson, PH; Londesborough, J; Penttilä, M; Richard, P; Sundqvist, L; Verho, R | 1 |
| Castilho, MS; Ladame, S; Oliva, G; Pavão, F; Périé, J; Willson, M | 1 |
| HILVERS, AG; SLATER, EC | 1 |
| FURFINE, CS; VELICK, SF | 1 |
| Belonje, B; Black, DB; Brooks, SP; Cockell, KA; Dawson, BA; Lampi, BJ; Plouffe, LJ; Ratnayake, WM | 1 |
| Bureau, MH; Griffon, N; Jeanneteau, F; Kurcewicz, I; Laschet, JJ; Louvel, J; Minier, F; Pumain, R; Samyn, B; Sokoloff, P; Trottier, S; Van Beeumen, J | 1 |
| Chattopadhyay, D; Cook, WJ; Senkovich, O | 1 |
| Gong, YJ; Kim, CW; Kim, SY; Koo, BS; Lee, HC | 1 |
| Cheong, GW; Jia, B; Lee, S; Linh, le T; Liu, J; Pan, H; Pham, BP; Zhang, S | 1 |
| Chishiki, H; Fushinobu, S; Ito, F; Wakagi, T | 1 |
| Li, H; Li, L; Liu, JP; Nicholls, C; Pinto, AR; Simpson, R; Wang, L | 1 |
| Hoey, EM; Timson, DJ; Trudgett, A; Zinsser, VL | 1 |
| Baker, BY; Palczewski, K; Shi, W; Wang, B | 1 |
| Bostrom, IK; Chen, AQ; Gu, SH; Ji, CN; Li, JX; Liu, MR; Wang, YD; Yao, YC; Zhang, L | 1 |
36 other study(ies) available for nad and glyceraldehyde 3-phosphate
| Article | Year |
|---|---|
Progress in establishing the rate-limiting features and kinetic mechanism of the glyceraldehyde-3-phosphate dehydrogenase reaction.
Topics: Arsenates; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen; Hydrogen-Ion Concentration; Kinetics; NAD | 1992 |
Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme-enzyme interaction. The example of 3-phospho-D-glycerate kinase and glyceraldehyde-3-phosphate dehydrogenase couple.
Topics: Animals; Catalysis; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Glyceric Acids; Kinetics; NAD; Phosphoglycerate Kinase; Swine | 1990 |
Inhibition of glyceraldehyde-3-phosphate dehydrogenase by pentalenolactone: kinetic and mechanistic studies.
Topics: Animals; Anti-Bacterial Agents; Binding, Competitive; Chromatography, Gel; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Muscles; NAD; Rabbits; Sesquiterpenes; Statistics as Topic; Sulfhydryl Reagents | 1989 |
D-glyceraldehyde-3-phosphate dehydrogenase subunit cooperativity studied using immobilized enzyme forms.
Topics: Allosteric Regulation; Animals; Diacetyl; Enzymes, Immobilized; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hot Temperature; Kinetics; Macromolecular Substances; Muscles; NAD; Rabbits; Structure-Activity Relationship; Sulfhydryl Compounds | 1988 |
Mechanism of glyceraldehyde-3-phosphate transfer from aldolase to glyceraldehyde-3-phosphate dehydrogenase.
Topics: Animals; Diphosphoglyceric Acids; Energy Transfer; Fructose-Bisphosphate Aldolase; Fructosediphosphates; Glyceraldehyde; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Models, Chemical; Muscles; NAD; Oxidative Phosphorylation; Rabbits | 1988 |
A simple approach to identify the mechanism of intermediate transfer: enzyme system related to triose phosphate metabolism.
Topics: Animals; Fructose-Bisphosphate Aldolase; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Muscles; NAD; Protein Conformation; Rabbits; Triose-Phosphate Isomerase | 1987 |
The content of pentose-cycle intermediates in liver in starved, fed ad libitum and meal-fed rats.
Topics: Animals; Diet; Fructosephosphates; Glyceraldehyde 3-Phosphate; Liver; Male; NAD; NADP; Oxidation-Reduction; Pentose Phosphate Pathway; Rats; Rats, Inbred Strains; Starvation | 1986 |
Regulation of glyceraldehyde-3-phosphate dehydrogenase by a cytosolic protein.
Topics: Adenosine Triphosphate; Animals; Cell Line; Chlorocebus aethiops; Cytosol; Enzyme Activation; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Kidney; Kinetics; NAD; Potassium; Proteins | 1985 |
Substrate-induced dissociation of glyceraldehyde-phosphate dehydrogenase detected by affinity chromatography. Study of subunit interactions by affinity sorption.
Topics: Animals; Chromatography, Affinity; Dextrans; Glyceraldehyde; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Macromolecular Substances; NAD; Rabbits; Spectrum Analysis | 1980 |
Actions of gamma-radiation on resealed erythrocyte ghosts. A comparison with intact erythrocytes and a study of the effects of oxygen.
Topics: Cell Membrane Permeability; Erythrocyte Membrane; Erythrocytes; Free Radicals; Gamma Rays; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Humans; In Vitro Techniques; NAD; Oxygen | 1981 |
The NADH-dependent transketolase assay: a note of caution.
Topics: Glyceraldehyde 3-Phosphate; Humans; NAD; Transketolase | 1982 |
Kinetic properties of NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from the host fraction of soybean root nodules.
Topics: Adenosine Monophosphate; Cytosol; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycine max; Kinetics; Models, Chemical; NAD; Nitrogen Fixation; Oxidation-Reduction; Oxidative Phosphorylation; Phosphates; Symbiosis | 1994 |
Functional significance of protein conformational isomerisation in the glyceraldehyde-3-phosphate dehydrogenase-catalysed reaction.
Topics: Catalysis; Fabaceae; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen-Ion Concentration; Isomerism; Kinetics; NAD; Oxidation-Reduction; Plant Proteins; Plants, Medicinal; Protein Conformation | 1993 |
Dependence on NADH produced during glycolysis for beta-cell glucose signaling.
Topics: Adenosine Triphosphate; Animals; Calcium; Cells, Cultured; Cytosol; Glucose; Glyceraldehyde 3-Phosphate; Glycolysis; Islets of Langerhans; Kinetics; Membrane Potentials; Mice; Mice, Inbred C57BL; Models, Biological; NAD; Niacinamide; Potassium Channels; Signal Transduction | 1994 |
D-glyceraldehyde-3-phosphate dehydrogenase: pre-existent asymmetry of the tetramer and its functional implications.
Topics: Animals; Binding Sites; Catalysis; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrolysis; Muscles; NAD; Protein Conformation; Rabbits; Structure-Activity Relationship | 1993 |
Glyceraldehyde-3-phosphate activates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase.
Topics: Adenosine Diphosphate Ribose; Aldehydes; Animals; Dithiothreitol; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Muscles; NAD; Nitroprusside; Rabbits; Substrate Specificity | 1993 |
Mechanism of inhibition of glycolysis in Streptococcus mutans NCIB 11723 by chlorhexidine.
Topics: Acetates; Adenosine Diphosphate; Adenosine Triphosphate; Anti-Infective Agents, Local; Cell Membrane Permeability; Chlorhexidine; Formates; Fructosediphosphates; Fructosephosphates; Glucose-6-Phosphate; Glucosephosphates; Glyceraldehyde 3-Phosphate; Glyceric Acids; Glycolysis; Intracellular Fluid; Lactates; NAD; Statistics, Nonparametric; Streptococcus mutans | 1995 |
The active site of phosphorylating glyceraldehyde-3-phosphate dehydrogenase is not designed to increase the nucleophilicity of a serine residue.
Topics: Amino Acid Substitution; Asparagine; Binding Sites; Enzyme Activation; Esters; Geobacillus stearothermophilus; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hot Temperature; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NAD; Phosphorylation; Protease Inhibitors; Serine; Tosyl Compounds | 1999 |
Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Carbon Isotopes; Corynebacterium; Fructosediphosphates; Glucosephosphate Dehydrogenase; Glutamate Dehydrogenase; Glyceraldehyde 3-Phosphate; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation; NAD; NADP; Pentose Phosphate Pathway; Phosphogluconate Dehydrogenase; Ribulosephosphates; Sugar Phosphates | 2000 |
Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli: direct evidence of substrate binding and cofactor-induced conformational changes.
Topics: Animals; Apoenzymes; Bacterial Proteins; Binding Sites; Computer Simulation; Crystallography, X-Ray; Escherichia coli; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Holoenzymes; Humans; Models, Molecular; NAD; Nephropidae; Protein Conformation; Structure-Activity Relationship; Substrate Specificity | 2000 |
Glycolytic enzyme activity in hypotonically treated boar spermatozoa.
Topics: Adenosine Diphosphate; Animals; Buffers; Dihydroxyacetone Phosphate; Fructosediphosphates; Glyceraldehyde 3-Phosphate; Glyceric Acids; Glycolysis; Hypotonic Solutions; L-Lactate Dehydrogenase; Lactic Acid; Male; NAD; Phosphates; Phosphofructokinase-1; Pyruvic Acid; Spermatozoa; Swine | 1999 |
The nicotinamide biosynthetic pathway is a by-product of the RNA world.
Topics: Aspartic Acid; Dihydroxyacetone; Dihydroxyacetone Phosphate; Glyceraldehyde; Glyceraldehyde 3-Phosphate; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Molecular Structure; NAD; Niacin; Quinolinic Acid; RNA | 2001 |
Identification of the first fungal NADP-GAPDH from Kluyveromyces lactis.
Topics: Amino Acid Sequence; Blotting, Northern; Cloning, Molecular; Galactose; Gene Library; Glucose; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating); Histidine; Kluyveromyces; Mitochondria; Molecular Sequence Data; Mutation; NAD; NADP; Phenotype; Phosphoglycerate Kinase; Plasmids; RNA, Messenger; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Transcription, Genetic; Xylose | 2002 |
Evidence for the two phosphate binding sites of an analogue of the thioacyl intermediate for the Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase-catalyzed reaction, from its crystal structure.
Topics: Acylation; Animals; Binding Sites; Catalysis; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Models, Molecular; NAD; Phosphates; Protein Conformation; Recombinant Proteins; Sulfhydryl Compounds; Trypanosoma cruzi | 2003 |
THE REACTION MECHANISM OF D-GLYCERALDEHYDE-3-PHOSPHATE:NAD+ OXIDOREDUCTASE (PHOSPHORYLATING) OF RABBIT MUSCLE.
Topics: Acetaldehyde; Alcohol Oxidoreductases; Aldehydes; Animals; Chemical Phenomena; Chemistry; Chromatography; Fructose-Bisphosphate Aldolase; Glyceraldehyde; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; L-Lactate Dehydrogenase; Muscles; N-Glycosyl Hydrolases; NAD; Neurospora; Oxidoreductases; Phosphates; Phosphoglycerate Kinase; Rabbits; Research; Spectrophotometry; Yeasts | 1964 |
THE ACYL-ENZYME INTERMEDIATE AND THE KINETIC MECHANISM OF THE GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE REACTION.
Topics: Arsenicals; Catalysis; Chemical Phenomena; Chemistry; Fluorometry; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen-Ion Concentration; Kinetics; NAD; Pyridines; Research; Spectrophotometry | 1965 |
Carbohydrate metabolism in erythrocytes of copper deficient rats.
Topics: Animals; Blood Glucose; Body Weight; Carbohydrates; Copper; Diet; Erythrocytes; Fructose; Glyceraldehyde 3-Phosphate; Glycolysis; Heart; Liver; Magnetic Resonance Spectroscopy; Male; NAD; Organ Size; Pentose Phosphate Pathway; Rats; Rats, Long-Evans; Superoxide Dismutase; Weaning | 2003 |
Glyceraldehyde-3-phosphate dehydrogenase is a GABAA receptor kinase linking glycolysis to neuronal inhibition.
Topics: Adenosine Diphosphate; Amino Acid Sequence; Animals; Brain Chemistry; Cattle; Cell Membrane; Chlorocebus aethiops; COS Cells; Diphosphates; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycolysis; Hippocampus; Iodoacetamide; Magnesium; Molecular Sequence Data; NAD; Neurons; Phosphorylation; Protein Interaction Mapping; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Rabbits; Rats; Rats, Sprague-Dawley; Receptors, GABA-A; Recombinant Fusion Proteins; Synaptic Transmission; Transfection | 2004 |
An unexpected phosphate binding site in glyceraldehyde 3-phosphate dehydrogenase: crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme.
Topics: Animals; Apoenzymes; Catalytic Domain; Cryptosporidium parvum; Escherichia coli; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Holoenzymes; Humans; Mutant Proteins; NAD; Protein Binding; Protein Conformation; Protozoan Proteins; Recombinant Proteins; X-Ray Diffraction | 2009 |
Improvement of coenzyme Q(10) production by increasing the NADH/NAD(+) ratio in Agrobacterium tumefaciens.
Topics: Agrobacterium tumefaciens; Culture Media; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; NAD; Ubiquinone | 2010 |
Biochemical characterization of glyceraldehyde-3-phosphate dehydrogenase from Thermococcus kodakarensis KOD1.
Topics: Amino Acid Sequence; Archaeal Proteins; Catalytic Domain; Cloning, Molecular; Diphosphoglyceric Acids; Enzyme Stability; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Half-Life; Hot Temperature; Kinetics; Microscopy, Electron, Transmission; Molecular Sequence Data; Molecular Weight; Mutation; NAD; Oxidative Stress; Protein Structure, Quaternary; Structure-Activity Relationship; Thermococcus | 2011 |
Comparative analysis of two glyceraldehyde-3-phosphate dehydrogenases from a thermoacidophilic archaeon, Sulfolobus tokodaii.
Topics: Archaeal Proteins; Base Sequence; DNA Primers; Enzyme Activation; Gluconeogenesis; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycolysis; Isoenzymes; Kinetics; Mutagenesis, Site-Directed; NAD; NADP; Oxidation-Reduction; Phosphorylation; Phylogeny; Recombinant Proteins; Substrate Specificity; Sulfolobus | 2012 |
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces cancer cell senescence by interacting with telomerase RNA component.
Topics: Breast Neoplasms; Cell Line, Tumor; Cellular Senescence; Female; Gene Expression Regulation, Neoplastic; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); Green Fluorescent Proteins; Humans; NAD; Protein Binding; Protein Structure, Tertiary; RNA; S-Nitrosoglutathione; Structure-Activity Relationship; Telomerase; Telomere Shortening | 2012 |
Biochemical characterisation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from the liver fluke, Fasciola hepatica.
Topics: Animals; Biocatalysis; Escherichia coli; Fasciola hepatica; Fluorometry; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Helminth Proteins; Humans; Kinetics; Models, Molecular; NAD; Protein Multimerization; Protein Stability; Recombinant Fusion Proteins | 2014 |
High-resolution crystal structures of the photoreceptor glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with three and four-bound NAD molecules.
Topics: Animals; Binding Sites; Catalytic Domain; Cattle; Crystallization; Glyceraldehyde 3-Phosphate; Models, Molecular; NAD; Protein Conformation; Retina | 2014 |
Characterization and structure of glyceraldehyde-3-phosphate dehydrogenase type 1 from Escherichia coli.
Topics: Amino Acid Sequence; Catalytic Domain; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Gene Expression; Genetic Vectors; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Humans; Models, Molecular; NAD; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Subunits; Recombinant Proteins; Shigella sonnei | 2020 |