glyphosate has been researched along with arginine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bauer, SC; Bild, GS; Borgmeyer, JR; Huynh, QK; Kishore, GM | 1 |
| Ahmad, S; Arora, N; Bhatnagar, RK; Fattah, FA; Majumder, K; Selvapandiyan, A | 1 |
| Cohen, ER; McDowell, LM; Schaefer, J; Schmidt, A; Studelska, DR | 1 |
| Chen, Y; Lin, Y; Liu, Z; Shao, Z; Wu, G; Yao, P; Zhan, T; Zhang, K; Zhang, L | 1 |
4 other study(ies) available for glyphosate and arginine
| Article | Year |
|---|---|
Site-directed mutagenesis of Petunia hybrida 5-enolpyruvylshikimate-3-phosphate synthase: Lys-23 is essential for substrate binding.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alanine; Alkyl and Aryl Transferases; Arginine; Binding Sites; Binding, Competitive; Glutamates; Glutamic Acid; Glycine; Glyphosate; Herbicides; Lysine; Mutation; Phosphoenolpyruvate; Plants; Pyridoxal Phosphate; Shikimic Acid; Transferases | 1988 |
Point mutation of a conserved arginine (104) to lysine introduces hypersensitivity to inhibition by glyphosate in the 5-enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases; Amino Acid Sequence; Arginine; Bacillus subtilis; Binding Sites; Conserved Sequence; Enzyme Inhibitors; Glutamine; Glycine; Glyphosate; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phosphoenolpyruvate; Point Mutation; Shikimic Acid; Substrate Specificity; Transferases | 1995 |
Structural constraints on the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase from rotational-echo double-resonance NMR.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases; Arginine; Binding Sites; Escherichia coli; Glycine; Glyphosate; Histidine; Lysine; Magnetic Resonance Spectroscopy; Molecular Structure; Nitrogen Isotopes; Shikimic Acid; Transferases | 1996 |
Improving glyphosate oxidation activity of glycine oxidase from Bacillus cereus by directed evolution.
Topics: Amino Acid Oxidoreductases; Amino Acid Substitution; Arginine; Bacillus cereus; Bacterial Proteins; Binding Sites; Binding, Competitive; Directed Molecular Evolution; Enzyme Stability; Glycine; Glyphosate; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Mutant Proteins; Mutation; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Substrate Specificity; Temperature | 2013 |