cytidine triphosphate has been researched along with glutamic acid in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kantrowitz, ER; Middleton, SA; Tauc, P; Vachette, P | 1 |
| Chan, RS; Kantrowitz, ER; Sakash, JB; Tsuruta, H | 1 |
| Goto, M; Hirotsu, K; Miyahara, I; Nakagawa, N; Omi, R | 1 |
| Mellors, JW; Parikh, UM; Sheen, CW; Sluis-Cremer, N; Torres, PS; Zelina, S | 1 |
4 other study(ies) available for cytidine triphosphate and glutamic acid
| Article | Year |
|---|---|
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 |
Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Aspartate Carbamoyltransferase; Catalytic Domain; Cytidine Triphosphate; Enzyme Stability; Escherichia coli; Glutamic Acid; Kinetics; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Proteins; X-Ray Diffraction | 2000 |
Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites.
Topics: Binding Sites; Carbon-Nitrogen Ligases; Crystallography, X-Ray; Cytidine Triphosphate; Glutamic Acid; Glutaminase; Guanosine Triphosphate; Models, Molecular; Thermus thermophilus; Uridine Triphosphate | 2004 |
Molecular mechanism by which the K70E mutation in human immunodeficiency virus type 1 reverse transcriptase confers resistance to nucleoside reverse transcriptase inhibitors.
Topics: Adenine; Amino Acid Substitution; Anti-HIV Agents; Cytidine Triphosphate; Dideoxynucleosides; Dideoxynucleotides; Drug Resistance, Multiple, Viral; Genotype; Glutamic Acid; HIV Reverse Transcriptase; HIV-1; Humans; Lamivudine; Lysine; Mutagenesis, Site-Directed; Organophosphonates; Phenotype; Reverse Transcriptase Inhibitors; Tenofovir; Thymine Nucleotides; Zidovudine | 2007 |