phosphonoacetic acid has been researched along with succinic acid in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (14.29) | 18.7374 |
| 1990's | 6 (85.71) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| East, JM; Lee, AG; Stefanova, HI | 1 |
| Cunin, R; Hervé, G; Ladjimi, MM; Van Vliet, F; Xi, XG | 1 |
| Kleanthous, C; Schachman, HK; Wemmer, DE | 1 |
| Kantrowitz, ER; Keiser, RT; Tauc, P; Vachette, P | 1 |
| Lum, L; Schachman, HK; Waldrop, GL; Zhou, BB | 1 |
| Baker, DP; Fetler, L; Kantrowitz, ER; Vachette, P | 1 |
| Burns, BP; Hazell, SL; Mendz, GL | 1 |
7 other study(ies) available for phosphonoacetic acid and succinic acid
| Article | Year |
|---|---|
Covalent and non-covalent inhibitors of the phosphate transporter of sarcoplasmic reticulum.
Topics: Acetic Anhydrides; Adenosine Triphosphatases; Animals; Binding Sites; Biological Transport; Calcium; Carrier Proteins; Female; Foscarnet; Maleates; Membrane Proteins; Muscles; Phenylglyoxal; Phosphate-Binding Proteins; Phosphates; Phosphonoacetic Acid; Rabbits; Sarcoplasmic Reticulum; Succinates; Succinic Acid | 1991 |
The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate.
Topics: Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Bacterial Proteins; Binding Sites; Carbamyl Phosphate; Catalysis; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Protein Binding; Substrate Specificity; Succinates; Succinic Acid | 1990 |
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Phosphonoacetic Acid; Succinates; Succinic Acid | 1988 |
Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.
Topics: Alanine; Allosteric Regulation; Allosteric Site; Aspartate Carbamoyltransferase; Aspartic Acid; Enzyme Activation; Enzyme Stability; Escherichia coli; Glutamic Acid; Kinetics; Nucleotides; Phosphonoacetic Acid; Point Mutation; Protein Conformation; Scattering, Radiation; Succinates; Succinic Acid; X-Rays | 1994 |
A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Carbon Isotopes; Catalysis; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Peptide Fragments; Phosphonoacetic Acid; Structure-Activity Relationship; Succinates; Succinic Acid; Zinc | 1994 |
The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Kinetics; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Protein Conformation; Scattering, Radiation; Succinates; Succinic Acid | 1996 |
In situ properties of Helicobacter pylori aspartate carbamoyltransferase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Enzyme Inhibitors; Helicobacter pylori; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Maleates; Organophosphates; Phosphonoacetic Acid; Ribose; Stereoisomerism; Substrate Specificity; Succinic Acid; Temperature | 1997 |