6-hydroxydopa quinone has been researched along with 4-nitrophenylhydrazine in 3 studies
Studies (6-hydroxydopa quinone) | Trials (6-hydroxydopa quinone) | Recent Studies (post-2010) (6-hydroxydopa quinone) | Studies (4-nitrophenylhydrazine) | Trials (4-nitrophenylhydrazine) | Recent Studies (post-2010) (4-nitrophenylhydrazine) |
---|---|---|---|---|---|
144 | 0 | 14 | 14 | 0 | 2 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (100.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Duine, JA; Groen, BW; Jongejan, JA; Niessen, WM; Steinebach, V; Wijmenga, SS | 1 |
Choi, YH; Matsuzaki, R; Nakamura, N; Sanders-Loehr, J; Tanizawa, K | 1 |
Adachi, O; Asano, Y; Frébort, I; Hirota, S; Kato, Y; Kitagawa, T; Luhová, L; Matsushita, K; Pec, P; Toyama, H; Ueno, T | 1 |
3 other study(ies) available for 6-hydroxydopa quinone and 4-nitrophenylhydrazine
Article | Year |
---|---|
Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase.
Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Consensus Sequence; Dihydroxyphenylalanine; Escherichia coli; Indicators and Reagents; Kidney; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Molecular Structure; Oxidoreductases Acting on CH-NH Group Donors; Phenylhydrazines; Spectrophotometry; Swine | 1995 |
Biosynthesis of topa quinone cofactor in bacterial amine oxidases. Solvent origin of C-2 oxygen determined by Raman spectroscopy.
Topics: Amine Oxidase (Copper-Containing); Amino Acid Oxidoreductases; Arthrobacter; Cloning, Molecular; Coenzymes; Copper; Dihydroxyphenylalanine; Escherichia coli; Indicators and Reagents; Isotope Labeling; Methylamines; Oxygen Isotopes; Phenylhydrazines; Recombinant Proteins; Solvents; Spectrum Analysis, Raman; Water | 1996 |
Two amine oxidases from Aspergillus niger AKU 3302 contain topa quinone as the cofactor: unusual cofactor link to the glutamyl residue occurs only at one of the enzymes.
Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Aspergillus niger; Coenzymes; Consensus Sequence; Dihydroxyphenylalanine; Glutamic Acid; Models, Chemical; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Peptide Fragments; Phenylhydrazines; Sequence Analysis | 1996 |