fructose 2,6-diphosphate has been researched along with arginine in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 4 (80.00) | 18.2507 |
| 2000's | 1 (20.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Fromm, HJ; Zhang, R | 1 |
| Giroux, E; Kantrowitz, ER; Williams, MK | 1 |
| Ambrosio, S; Bartrons, R; Bendahan, G; Calopa, M; Espino, A; Ferrer, I; Tortosa, A | 1 |
| Gunasekera, D; Kemp, RG; Li, Y; Rivera, D; Ru, W | 1 |
| Enomoto, T; Nakao, C; Ohyama, H | 1 |
5 other study(ies) available for fructose 2,6-diphosphate and arginine
| Article | Year |
|---|---|
Mutation of arginine 276 to methionine changes Mg2+ cooperativity and the kinetic mechanism of fructose-1,6-bisphosphatase.
Topics: Adenosine Monophosphate; Animals; Arginine; Base Sequence; Electrophoresis, Polyacrylamide Gel; Fructose-Bisphosphatase; Fructosediphosphates; Kinetics; Liver; Magnesium; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Structure-Activity Relationship; Swine | 1995 |
Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition.
Topics: Adenosine Monophosphate; Animals; Arginine; Binding Sites; Catalysis; Fructose-Bisphosphatase; Fructosediphosphates; In Vitro Techniques; Kinetics; Magnesium; Models, Molecular; Mutagenesis, Site-Directed; Structure-Activity Relationship; Swine | 1994 |
Stereotaxic administration of 1-methyl-4-phenylpyridinium ion (MPP+) decreases striatal fructose 2,6-bisphosphate in rats.
Topics: 1-Methyl-4-phenylpyridinium; Adenine Nucleotides; Animals; Arginine; Dizocilpine Maleate; Fructosediphosphates; Glycolysis; Hexosephosphates; Kinetics; Male; Neostriatum; Nitroarginine; Rats; Rats, Sprague-Dawley; Rotenone; Stereotaxic Techniques; Time Factors | 1994 |
Identification of allosteric sites in rabbit phosphofructo-1-kinase.
Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Allosteric Site; Animals; Arginine; Enzyme Activators; Enzyme Inhibitors; Escherichia coli; Fructosediphosphates; Geobacillus stearothermophilus; Leucine; Mutagenesis, Site-Directed; Phosphofructokinase-1; Point Mutation; Rabbits | 1999 |
Regulation of glycolysis during acclimation of scallops (Patinopecten yessoensis Jay) to anaerobiosis.
Topics: Adenosine Triphosphate; Animals; Arginine; Fermentation; Fructosediphosphates; Fructosephosphates; Glucose-6-Phosphate; Glycolysis; Hypoxia; Mollusca; Oxygen; Oxygen Consumption; Phosphofructokinase-1; Time Factors | 2000 |