trimetrexate and nadp
trimetrexate has been researched along with nadp in 5 studies
Research
Studies (5)
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (20.00) | 18.7374 |
| 1990's | 2 (40.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 2 (40.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Authors
| Authors | Studies |
|---|---|
| Allegra, CJ; Chabner, BA; Drake, JC; Kovacs, JA; Masur, H; Swan, JC | 1 |
| Briand, CM; Gilli, RM; Rimet, OS; Sari, JC; Sasso, SP | 1 |
| Briand, C; Gilli, R; Lopez, C; Sari, JC; Sasso, S | 1 |
| Barrack, KL; Dawson, A; Hunter, WN; Tulloch, LB | 1 |
| Cheng, YS; Sacchettini, JC | 1 |
Other Studies
5 other study(ies) available for trimetrexate and nadp
| Article | Year |
|---|---|
Activity of antifolates against Pneumocystis carinii dihydrofolate reductase and identification of a potent new agent.
Topics: Biological Transport; Folic Acid Antagonists; Kinetics; Methotrexate; NADP; Pneumocystis; Quinazolines; Tetrahydrofolate Dehydrogenase; Trimetrexate | 1987 |
Thermodynamic study of dihydrofolate reductase inhibitor selectivity.
Topics: Animals; Escherichia coli; Folic Acid Antagonists; Methotrexate; Mice; NADP; Protein Folding; Temperature; Thermodynamics; Trimethoprim; Trimetrexate | 1994 |
Thermodynamic study of folate analogue binding to dihydrofolate reductases from different species.
Topics: Animals; Calorimetry; Cattle; Escherichia coli; Folic Acid Antagonists; Liver; Methotrexate; NADP; Oxidation-Reduction; Species Specificity; Tetrahydrofolate Dehydrogenase; Thermodynamics; Trimethoprim; Trimetrexate | 1993 |
High-resolution structures of Trypanosoma brucei pteridine reductase ligand complexes inform on the placement of new molecular entities in the active site of a potential drug target.
Topics: Catalytic Domain; Crystallography, X-Ray; Glutamates; Guanine; Ligands; Models, Molecular; NADP; Oxidoreductases; Pemetrexed; Protein Binding; Triazines; Trimetrexate; Trypanosoma brucei brucei | 2010 |
Structural Insights into Mycobacterium tuberculosis Rv2671 Protein as a Dihydrofolate Reductase Functional Analogue Contributing to para-Aminosalicylic Acid Resistance.
Topics: Aminosalicylic Acid; Antitubercular Agents; Bacterial Proteins; Catalytic Domain; Drug Resistance, Bacterial; Enzyme Inhibitors; Folic Acid Antagonists; Kinetics; Ligands; Models, Molecular; Molecular Conformation; Mycobacterium tuberculosis; NADP; Nucleotide Deaminases; Phylogeny; Recombinant Proteins; Tetrahydrofolate Dehydrogenase; Tetrahydrofolates; Trimethoprim; Trimetrexate | 2016 |