arginine has been researched along with thymidine monophosphate in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (40.00) | 18.7374 |
| 1990's | 1 (20.00) | 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 |
|---|---|
| Cipollo, KL; Dunlap, RB | 1 |
| Andini, S; Bonora, GM; Ferrara, L; Paolillo, L; Toniolo, C; Wurzburger, S | 1 |
| Connolly, BA; Doherty, AJ; Worrall, AF | 1 |
| Lee, TT; Liu, Y; Santi, DV; Stroud, RM; Variath, P | 1 |
| Changchien, L; Maley, F; Montfort, WR; Sotelo-Mundo, RR | 1 |
5 other study(ies) available for arginine and thymidine monophosphate
| Article | Year |
|---|---|
Essential arginyl residues in thymidylate synthetase.
Topics: Arginine; Binding Sites; Deoxyuracil Nucleotides; Diacetyl; Folic Acid; Kinetics; Lacticaseibacillus casei; Methyltransferases; Thymidine Monophosphate; Thymidylate Synthase | 1978 |
Nuclear magnetic resonance of protamines. A 1H-NMR study of the interaction of clupeine fractions with mononucleotides.
Topics: Adamantane; Amino Acid Sequence; Arginine; Clupeine; Deoxycytidine Monophosphate; Deoxyguanine Nucleotides; Magnetic Resonance Spectroscopy; Nucleotides; Protamines; Salmine; Thymidine Monophosphate | 1986 |
The roles of arginine 41 and tyrosine 76 in the coupling of DNA recognition to phosphodiester bond cleavage by DNase I: a study using site-directed mutagenesis.
Topics: Animals; Arginine; Base Sequence; Cattle; Deoxyribonuclease I; DNA; Escherichia coli; Hydrogen Bonding; Hydrolysis; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Phosphoric Diester Hydrolases; Promoter Regions, Genetic; Substrate Specificity; Thymidine Monophosphate; Tyrosine | 1995 |
Effects of subunit occupancy on partitioning of an intermediate in thymidylate synthase mutants.
Topics: Alanine; Arginine; Catalysis; Deoxyuracil Nucleotides; Escherichia coli; Glycine; Kinetics; Lacticaseibacillus casei; Models, Chemical; Mutagenesis, Site-Directed; Peptide Fragments; Tetrahydrofolates; Thymidine Monophosphate; Thymidylate Synthase; Valine | 2000 |
Crystal structures of thymidylate synthase mutant R166Q: structural basis for the nearly complete loss of catalytic activity.
Topics: Amino Acid Substitution; Arginine; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Deoxyuracil Nucleotides; Dimerization; Escherichia coli; Folic Acid; Folic Acid Antagonists; Hydrogen Bonding; Kinetics; Ligands; Models, Molecular; Molecular Structure; Protein Binding; Protein Conformation; Recombinant Proteins; Thymidine Monophosphate; Thymidylate Synthase | 2006 |