arginine has been researched along with fructose-1,6-diphosphate in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (25.00) | 18.7374 |
| 1990's | 5 (62.50) | 18.2507 |
| 2000's | 1 (12.50) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Koide, S; Matsuzawa, H; Miyazawa, T; Ohta, T; Yokoyama, S | 1 |
| Atkinson, T; Barstow, DA; Chia, WN; Clarke, AR; Holbrook, JJ; Wigley, DB | 1 |
| Depré, C; Hue, L | 1 |
| Giroux, E; Kantrowitz, ER; Williams, MK | 1 |
| Davenport, RC; Morris, AJ; Tolan, DR | 1 |
| Preiss, J; Sheng, J | 1 |
| Bystrom, CE; Ormö, M; Remington, SJ | 1 |
| Enomoto, T; Nakao, C; Ohyama, H | 1 |
8 other study(ies) available for arginine and fructose-1,6-diphosphate
| Article | Year |
|---|---|
Conformation of NAD+ bound to allosteric L-lactate dehydrogenase activated by chemical modification.
Topics: Allosteric Regulation; Allosteric Site; Arginine; Butanones; Diacetyl; Fructosediphosphates; Hexosediphosphates; Kinetics; L-Lactate Dehydrogenase; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; NAD; Thermus | 1989 |
A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure.
Topics: Allosteric Regulation; Allosteric Site; Arginine; Bacterial Proteins; Binding Sites; Fructosediphosphates; Geobacillus stearothermophilus; Glutamine; L-Lactate Dehydrogenase; Mutation; NAD; Protein Binding; Protein Conformation; Pyruvates; Pyruvic Acid | 1987 |
Cyclic GMP in the perfused rat heart. Effect of ischaemia, anoxia and nitric oxide synthase inhibitor.
Topics: Adenosine Triphosphate; Amino Acid Oxidoreductases; Animals; Arginine; Coronary Circulation; Cyclic GMP; Fructosediphosphates; Glucose; Glycogen; Heart; Hexosephosphates; Hypoxia; In Vitro Techniques; Kinetics; Male; Myocardial Ischemia; Myocardium; NG-Nitroarginine Methyl Ester; Nitric Oxide Synthase; Perfusion; Rats; Rats, Wistar; Time Factors | 1994 |
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 |
A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation.
Topics: Animals; Arginine; Binding Sites; Borohydrides; Circular Dichroism; Escherichia coli; Fructose-Bisphosphate Aldolase; Fructosediphosphates; Kinetics; Lysine; Mutagenesis, Site-Directed; Point Mutation; Protein Engineering; Rabbits; Schiff Bases | 1996 |
Arginine294 is essential for the inhibition of Anabaena PCC 7120 ADP-glucose pyrophosphorylase by phosphate.
Topics: Adenosine Triphosphate; Alanine; Amino Acid Substitution; Anabaena; Arginine; Binding Sites; Fructosediphosphates; Glucose-1-Phosphate Adenylyltransferase; Glyceric Acids; Kinetics; Mutagenesis, Site-Directed; Nucleotidyltransferases; Phenylglyoxal; Phosphates; Pyridoxal Phosphate; Recombinant Proteins | 1997 |
Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate.
Topics: Alanine; Allosteric Regulation; Arginine; Binding Sites; Chromatography, Gel; Crystallization; Crystallography, X-Ray; Escherichia coli; Fructosediphosphates; Glycerol Kinase; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Solutions | 1998 |
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 |