carbamyl phosphate has been researched along with cytidine triphosphate in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (27.27) | 18.7374 |
| 1990's | 7 (63.64) | 18.2507 |
| 2000's | 1 (9.09) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hunston, DL; Klotz, IM | 1 |
| Kantrowitz, ER; Newton, CJ; Stevens, RC | 1 |
| Cleland, WW; O'Leary, MH; Parmentier, LE; Schachman, HK | 1 |
| Schachman, HK; Wente, SR | 1 |
| Kantrowitz, ER; Middleton, SA; Tauc, P; Vachette, P | 1 |
| Eisenstein, E; Markby, DW; Schachman, HK | 1 |
| Hsuanyu, YC; Kantrowitz, ER; Middleton, SA; Wedler, FC | 1 |
| Hervé, G; Jones, PT; Moody, MF; Tauc, P; Vachette, P | 1 |
| Baker, DP; Fetler, L; Kantrowitz, ER; Keiser, RT; Vachette, P | 1 |
| Burns, BP; Hazell, SL; Mendz, GL | 1 |
| Cunin, R; Maes, D; Van Boxstael, S | 1 |
11 other study(ies) available for carbamyl phosphate and cytidine triphosphate
| Article | Year |
|---|---|
Analytical and graphical examination of strong binding by half-of-sites in proteins: illustration with aspartate transcarbamylase.
Topics: Aspartate Carbamoyltransferase; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; Models, Biological; Protein Binding | 1977 |
Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Computer Simulation; Cytidine Triphosphate; Escherichia coli; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Structure-Activity Relationship | 1992 |
13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Carbon Isotopes; Cysteine; Cytidine Triphosphate; Escherichia coli; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Macromolecular Substances; Neurotransmitter Agents | 1992 |
Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; DNA Mutational Analysis; Histidine; Lysine; Phosphonoacetic Acid; Structure-Activity Relationship | 1991 |
Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Glutamates; Glutamic Acid; Glutamine; Phosphonoacetic Acid; Protein Engineering; Structure-Activity Relationship; X-Ray Diffraction | 1990 |
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Kinetics; Mutation; Phosphonoacetic Acid; Protein Conformation | 1990 |
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 |
Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding.
Topics: Adenosine Triphosphate; Allosteric Site; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Macromolecular Substances; Phosphonoacetic Acid; X-Rays | 1985 |
Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Kinetics; Mutagenesis; Point Mutation; Protein Conformation; Scattering, Radiation; Structure-Activity Relationship; Substrate Specificity; Succinates; Succinic Acid; Uridine Triphosphate; X-Rays | 1995 |
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 |
Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi. Insights into cooperative and allosteric mechanisms.
Topics: Adenosine Triphosphate; Allosteric Regulation; Allosteric Site; Aspartate Carbamoyltransferase; Carbamoyl-Phosphate Synthase (Ammonia); Carbamyl Phosphate; Catalysis; Cytidine Triphosphate; Escherichia coli; Phosphonoacetic Acid; Pyrococcus abyssi; Recombinant Proteins; Uridine Triphosphate | 2005 |