glycerate 1,3-biphosphate has been researched along with nad in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 4 (80.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Kvassman, J; Pettersson, G | 2 |
Kvassman, J; Pettersson, G; Ryde-Pettersson, U | 1 |
Oberdisse, E; Rosenthal, W; Weber, G | 1 |
Cheong, GW; Jia, B; Lee, S; Linh, le T; Liu, J; Pan, H; Pham, BP; Zhang, S | 1 |
5 other study(ies) available for glycerate 1,3-biphosphate and nad
Article | Year |
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Evidence that 1,3-bisphosphoglycerate dissociation from phosphoglycerate kinase is an intrinsically rapid reaction step.
Topics: Adenosine Triphosphate; Animals; Diphosphoglyceric Acids; Flatfishes; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; NAD; Phosphoglycerate Kinase | 1989 |
Mechanism of 1,3-bisphosphoglycerate transfer from phosphoglycerate kinase to glyceraldehyde-3-phosphate dehydrogenase.
Topics: Animals; Catalysis; Diphosphoglyceric Acids; Flatfishes; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; NAD; Phosphoglycerate Kinase | 1989 |
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 radiometric method for the determination of NADH in subpicomole amounts.
Topics: Adenosine Triphosphate; Diphosphoglyceric Acids; Glyceraldehyde-3-Phosphate Dehydrogenases; Glyceric Acids; Hydrogen-Ion Concentration; Microchemistry; NAD; Phosphates; Phosphoglycerate Kinase; Phosphorus Radioisotopes; Radiometry | 1988 |
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 |