aspartic acid has been researched along with fructose-1,6-diphosphate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Auzat, I; Garel, JR | 1 |
| Atkinson, T; Cortés, A; Gelpi, JL; Holbrook, JJ; Nicholls, DJ; Nobbs, TJ; Scawen, MD | 1 |
| Dodds, DC; Pettigrew, DW; Smith, GB; Thomas, KP | 1 |
| Chen, LM; Hata, S; Izui, K; Omiya, T | 1 |
4 other study(ies) available for aspartic acid and fructose-1,6-diphosphate
| Article | Year |
|---|---|
pH dependence of the reverse reaction catalyzed by phosphofructokinase I from Escherichia coli: implications for the role of Asp 127.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aspartic Acid; Catalysis; Escherichia coli; Fructosediphosphates; Fructosephosphates; Hydrogen-Ion Concentration; Models, Biological; Models, Chemical; Phosphofructokinase-1 | 1992 |
Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase.
Topics: Aspartic Acid; Catalysis; Enzyme Stability; Fructosediphosphates; Geobacillus stearothermophilus; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; L-Lactate Dehydrogenase; Molecular Sequence Data; Oligodeoxyribonucleotides; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Temperature | 1994 |
Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily.
Topics: Allosteric Regulation; Allosteric Site; Amino Acid Sequence; Asparagine; Aspartic Acid; Binding Sites; Conserved Sequence; Escherichia coli; Escherichia coli Proteins; Fructosediphosphates; Glycerol Kinase; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate Sugar Phosphotransferase System; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins | 1998 |
Molecular characterization of a phosphoenolpyruvate carboxylase from a thermophilic cyanobacterium, Synechococcus vulcanus with unusual allosteric properties.
Topics: Allosteric Regulation; Amino Acid Sequence; Aspartic Acid; Cloning, Molecular; Cyanobacteria; Escherichia coli; Fructosediphosphates; Gene Expression; Genes, Bacterial; Genomic Library; Glyceric Acids; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Malates; Molecular Sequence Data; Phosphoenolpyruvate; Phosphoenolpyruvate Carboxylase; Restriction Mapping; Sequence Homology, Amino Acid | 2002 |