phenylalanine has been researched along with carbamyl phosphate in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (60.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (40.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hsuanyu, Y; Kantrowitz, ER; Middleton, SA; Wedler, FC | 1 |
| Hsuanyu, YC; Kantrowitz, ER; Middleton, SA; Wedler, FC | 1 |
| Bookchin, RM; Chang, H; Ewert, SM; Nagel, RL | 1 |
| Huang, X; Raushel, FM | 1 |
| Bush, JA; Davis, TA; Nguyen, HV; Suryawan, A; Wu, G | 1 |
1 review(s) available for phenylalanine and carbamyl phosphate
| Article | Year |
|---|---|
Comparative evaluation of fifteen anti-sickling agents.
Topics: Anemia, Sickle Cell; Antisickling Agents; Aspirin; Azepines; Carbamyl Phosphate; Cyanates; Cystamine; Dimethyl Adipimidate; Drug Evaluation; Erythrocyte Indices; Glyceraldehyde; Hemoglobins; Humans; Imidoesters; Mechlorethamine; Oxygen Consumption; Phenylalanine; Pyridoxal; Solubility; Urea | 1983 |
4 other study(ies) available for phenylalanine and carbamyl phosphate
| Article | Year |
|---|---|
Site-specific mutation of Tyr240----Phe in the catalytic chain of Escherichia coli aspartate transcarbamylase. Consequences for kinetic mechanism.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Catalysis; Computer Simulation; Escherichia coli; Kinetics; Mutation; Phenylalanine; Phosphates; Protein Conformation; Structure-Activity Relationship; Thermodynamics; Tyrosine | 1989 |
Regulatory behavior of Escherichia coli aspartate transcarbamylase altered by site-specific mutation of Tyr240----Phe in the catalytic chain.
Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Catalysis; Computer Simulation; Cytidine Triphosphate; Enzyme Activation; Escherichia coli; Kinetics; Mutation; Phenylalanine; Phosphates; Structure-Activity Relationship; Thermodynamics; Tyrosine | 1989 |
An engineered blockage within the ammonia tunnel of carbamoyl phosphate synthetase prevents the use of glutamine as a substrate but not ammonia.
Topics: Alanine; Ammonia; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; Escherichia coli; Glutamic Acid; Glutamine; Glycine; Kinetics; Lysine; Methionine; Mutagenesis, Site-Directed; Phenylalanine; Serine; Substrate Specificity; Time Factors | 2000 |
Somatotropin-induced amino acid conservation in pigs involves differential regulation of liver and gut urea cycle enzyme activity.
Topics: Amino Acids; Ammonia; Animals; Bicarbonates; Blood Urea Nitrogen; Body Weight; Breath Tests; Carbamyl Phosphate; Carbon Isotopes; Female; Glutamates; Growth Hormone; Jejunum; Liver; Nitrogen; Oxidation-Reduction; Phenylalanine; Random Allocation; Substrate Specificity; Swine; Urea | 2002 |