6-hydroxydopa quinone has been researched along with asparagine in 2 studies
| Studies (6-hydroxydopa quinone) | Trials (6-hydroxydopa quinone) | Recent Studies (post-2010) (6-hydroxydopa quinone) | Studies (asparagine) | Trials (asparagine) | Recent Studies (post-2010) (asparagine) |
|---|---|---|---|---|---|
| 144 | 0 | 14 | 6,819 | 41 | 1,398 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (50.00) | 18.2507 |
| 2000's | 1 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Green, EL; Klinman, JP; Sanders-Loehr, J; Schwartz, B | 1 |
| Dove, JE; Klinman, JP; Schwartz, B; Williams, NK | 1 |
2 other study(ies) available for 6-hydroxydopa quinone and asparagine
| Article | Year |
|---|---|
Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast.
Topics: Alanine; Amine Oxidase (Copper-Containing); Amino Acid Sequence; Asparagine; Catalysis; Coenzymes; Conserved Sequence; Dihydroxyphenylalanine; Enzyme Activation; Kinetics; Methylamines; Mutagenesis, Site-Directed; Pichia; Protein Conformation; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet; Temperature | 1998 |
Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast.
Topics: Amine Oxidase (Copper-Containing); Asparagine; Aspartic Acid; Binding Sites; Coenzymes; Copper; Cysteine; Dihydroxyphenylalanine; Glutamic Acid; Glutamine; Histidine; Mutagenesis, Site-Directed; Oxygen Consumption; Pichia; Recombinant Proteins; Spectrophotometry, Atomic; Spectrophotometry, Ultraviolet | 2000 |