phenylalanine has been researched along with 2-hydrazinopyridine in 2 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Knowles, PF; Kurtis, CR; McPherson, MJ; Murray, JM; Parsons, MR; Phillips, SE; Saysell, CG; Tambyrajah, W; Wilmot, CM | 1 |
| Brown, DE; Dooley, DM; Knowles, PF; Kurtis, CR; McPherson, MJ; Mure, M; Phillips, SE; Rogers, MS; Saysell, C; Tambyrajah, WS; Wilmot, CM | 1 |
2 other study(ies) available for phenylalanine and 2-hydrazinopyridine
| Article | Year |
|---|---|
Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
Topics: Amine Oxidase (Copper-Containing); Binding Sites; Conserved Sequence; Crystallography, X-Ray; Dimerization; Electrons; Enzyme Inhibitors; Escherichia coli; Hydrogen; Hydrogen-Ion Concentration; Kinetics; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Protein Binding; Protein Conformation; Pyridones; Spectrophotometry; Time Factors; Tyrosine; Ultraviolet Rays | 2001 |
Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct.
Topics: Amine Oxidase (Copper-Containing); Asparagine; Aspartic Acid; Azo Compounds; Binding Sites; Cations, Divalent; Chelating Agents; Cobalt; Copper; Crystallography, X-Ray; Enzyme Inhibitors; Enzyme Stability; Escherichia coli Proteins; Glutamic Acid; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Phenylalanine; Pyridones; Resorcinols; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tyrosine | 2005 |