phosphonoacetic acid has been researched along with carbamyl phosphate in 26 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 12 (46.15) | 18.7374 |
| 1990's | 12 (46.15) | 18.2507 |
| 2000's | 2 (7.69) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Allwell, NM; Hofmann, GE; Lennick, M; Zaug, A | 1 |
| Allewell, NM; Knier, BL | 1 |
| Balfe, CA; Buttlaire, DH; Himes, RH; Wendland, MF | 1 |
| Ackerhalt, R; Blau, M; Kung, HF | 1 |
| Goldin, A; Inouye, T; Johnson, RK; Stark, GR | 1 |
| Kantrowitz, ER; Newton, CJ; Stevens, RC | 1 |
| Schachman, HK; Turnbull, JL; Waldrop, GL | 1 |
| Cleland, WW; Lee, S; O'Leary, MH; Parmentier, LE; Schachman, HK; Turnbull, JL; Waldrop, GL | 1 |
| Schachman, HK; Wente, SR | 1 |
| Kantrowitz, ER; Middleton, SA; Tauc, P; Vachette, P | 1 |
| Eisenstein, E; Markby, DW; Schachman, HK | 1 |
| Cunin, R; Hervé, G; Ladjimi, MM; Van Vliet, F; Xi, XG | 1 |
| Kantrowitz, ER; Xu, W | 1 |
| Kleanthous, C; Schachman, HK; Wemmer, DE | 1 |
| Gouaux, JE; Krause, KL; Lipscomb, WN | 1 |
| Hervé, G; Jones, PT; Moody, MF; Tauc, P; Vachette, P | 1 |
| Farrington, GK; Kumar, A; Wedler, FC | 1 |
| Yon, RJ | 1 |
| Christopherson, RI; Duggleby, RG | 1 |
| Burns, CM; Chernov, MV; Ishizaka, Y; Stark, GR | 1 |
| Allewell, NM; Bromberg, S; LiCata, VJ; Mallikarachchi, D | 1 |
| Lum, L; Schachman, HK; Waldrop, GL; Zhou, BB | 1 |
| Burns, BP; Hazell, SL; Mendz, GL | 1 |
| Evans, D; Guy, H; Hervé, G; Lux, M; Penverne, B; Rotgeri, A; Serre, V | 1 |
| Davidson, JN; Qiu, Y | 1 |
| Cunin, R; Maes, D; Van Boxstael, S | 1 |
26 other study(ies) available for phosphonoacetic acid and carbamyl phosphate
| Article | Year |
|---|---|
Bohr effect in Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Calorimetry; Carbamyl Phosphate; Escherichia coli; Hydrogen-Ion Concentration; Oxyhemoglobins; Phosphonoacetic Acid; Potentiometry; Protein Conformation; Protons; Spectrophotometry; Succinates | 1979 |
Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of substrates and substrate analogues to the native enzyme and catalytic subunit.
Topics: Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Calorimetry; Carbamyl Phosphate; Escherichia coli; Macromolecular Substances; Phosphonoacetic Acid; Protein Conformation; Thermodynamics | 1978 |
Carbamyl phosphate-dependent ATP synthesis catalyzed by formyltetrahydrofolate synthetase.
Topics: Acetates; Adenosine Diphosphate; Adenosine Triphosphate; Carbamates; Carbamyl Phosphate; Clostridium; Formate-Tetrahydrofolate Ligase; Formyltetrahydrofolates; Kinetics; Ligases; Organophosphorus Compounds; Phosphates; Phosphonoacetic Acid; Potassium; Tetrahydrofolates | 1979 |
Uptake of Tc-99m monophosphate complexes in bone and myocardial necrosis in animals.
Topics: Animals; Bone and Bones; Carbamyl Phosphate; Cardiomyopathies; Disease Models, Animal; Organophosphorus Compounds; Phosphonoacetic Acid; Rabbits; Rats; Technetium | 1978 |
Antitumor activity of N-(phosphonacetyl)-L-aspartic acid, a transition-state inhibitor of aspartate transcarbamylase.
Topics: Animals; Antineoplastic Agents; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Drug Administration Schedule; Female; Leukemia L1210; Leukemia, Experimental; Lung Neoplasms; Male; Melanoma; Mice; Neoplasms, Experimental; Organophosphorus Compounds; Osteosarcoma; Phosphonoacetic Acid | 1976 |
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 |
Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase.
Topics: Amino Acids; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Carbon Radioisotopes; Catalysis; Escherichia coli; Hydrogen-Ion Concentration; Ions; Kinetics; Phosphonoacetic Acid; Recombinant Proteins | 1992 |
The contribution of threonine 55 to catalysis in aspartate transcarbamoylase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Base Sequence; Carbamyl Phosphate; Carbon Isotopes; Catalysis; Deuterium; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrogen Isotopes; Oligonucleotides; Phosphonoacetic Acid; Structure-Activity Relationship; Succinates; Threonine | 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 |
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 |
Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase.
Topics: Alanine; Antineoplastic Agents; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Escherichia coli; Kinetics; Molecular Structure; Mutation; Phosphonoacetic Acid; Protein Conformation; Threonine | 1989 |
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 |
The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Chemical Phenomena; Chemistry; Escherichia coli; Hydrogen Bonding; Models, Chemical; Molecular Conformation; Phosphonoacetic Acid | 1987 |
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 |
Design and synthesis of new transition-state analogue inhibitors of aspartate transcarbamylase.
Topics: Antimetabolites, Antineoplastic; Aspartate Carbamoyltransferase; Aspartic Acid; Binding, Competitive; Carbamyl Phosphate; Chemical Phenomena; Chemistry; Kinetics; Organophosphorus Compounds; Organothiophosphorus Compounds; Phosphonoacetic Acid; Structure-Activity Relationship | 1985 |
Regulatory kinetics of wheat-germ aspartate transcarbamoylase. Adaptation of the concerted model to account for complex kinetic effects of uridine 5'-monophosphate.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Kinetics; Models, Chemical; Phosphonoacetic Acid; Plants; Protein Conformation; Triticum; Uracil Nucleotides; Uridine Monophosphate | 1984 |
Metabolic resistance: the protection of enzymes against drugs which are tight-binding inhibitors by the accumulation of substrate.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Drug Resistance; Models, Chemical; Orotidine-5'-Phosphate Decarboxylase; Phosphonoacetic Acid | 1983 |
p53-dependent growth arrest of REF52 cells containing newly amplified DNA.
Topics: Animals; Antigens, Viral, Tumor; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cell Cycle; Cell Line; Cyclin-Dependent Kinase Inhibitor p21; Cyclins; Dihydroorotase; DNA Damage; DNA Replication; Drug Resistance; Gene Amplification; Hot Temperature; In Situ Hybridization, Fluorescence; Ligases; Mutation; Phosphonoacetic Acid; Rats; Recombinant Proteins; RNA, Messenger; Selection, Genetic; Simian virus 40; Tumor Suppressor Protein p53 | 1995 |
Ligation alters the pathway of urea-induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Anions; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Catalysis; Chemical Phenomena; Chemistry, Physical; Chlorides; Escherichia coli; Macromolecular Substances; Phosphonoacetic Acid; Protein Denaturation; Protein Folding; Spectrophotometry; Thermodynamics; Urea | 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 |
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 |
Half of Saccharomyces cerevisiae carbamoyl phosphate synthetase produces and channels carbamoyl phosphate to the fused aspartate transcarbamoylase domain.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; Feedback; Multienzyme Complexes; Phosphonoacetic Acid; Phosphotransferases (Carboxyl Group Acceptor); Plasmids; Pyrimidines; Saccharomyces cerevisiae; Uridine Triphosphate | 1999 |
Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure.
Topics: Animals; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; CHO Cells; Cricetinae; Dihydroorotase; Encephalomyocarditis virus; Molecular Structure; Multienzyme Complexes; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Plasmids; Protein Conformation; Transfection | 2000 |
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 |