phenylhydrazine has been researched along with 6-hydroxydopa quinone in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 4 (44.44) | 18.2507 |
| 2000's | 4 (44.44) | 29.6817 |
| 2010's | 1 (11.11) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brown, DE; Dooley, DM; Janes, SM; Klinman, JP; Mure, M; Palcic, MM; Scaman, CH; Smith, AJ | 1 |
| Choi, YH; Fukui, T; Matsuzaki, R; Ozaki, Y; Sato, H; Shimizu, E; Tanizawa, K; Yorifuji, T | 1 |
| Choi, YH; Matsuzaki, R; Suzuki, S; Tanizawa, K | 1 |
| Agostinelli, E; De Matteis, G; Mondovì, B; Morpurgo, L; Sinibaldi, A | 1 |
| Agostinelli, E; Bellelli, A; Mondovì, B; Morpurgo, L | 1 |
| Bollinger, JA; Dooley, DM; Elmore, BO | 1 |
| Dooley, DM; Elmore, BO; Kuchar, JA; Sayre, LM; Shepard, EM; Smith, J | 1 |
| DuBois, JL; Klinman, JP | 1 |
| Altmann, F; Boehm, T; Bonta, M; Borth, N; Furtmüller, PG; Gludovacz, E; Jilma, B; Limbeck, A; Maresch, D; Szöllösi, H; Weik, R | 1 |
9 other study(ies) available for phenylhydrazine and 6-hydroxydopa quinone
| Article | Year |
|---|---|
Identification of topaquinone and its consensus sequence in copper amine oxidases.
Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Binding Sites; Chromatography, High Pressure Liquid; Coenzymes; Consensus Sequence; Dihydroxyphenylalanine; Fabaceae; Kidney; Molecular Sequence Data; Peptide Fragments; Phenylhydrazines; Plants, Medicinal; Spectrum Analysis, Raman; Swine; Trypsin | 1992 |
Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme, and generation of topa quinone cofactor.
Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Arthrobacter; Base Sequence; Cloning, Molecular; Copper; Dihydroxyphenylalanine; DNA, Bacterial; Enzyme Activation; Enzyme Precursors; Molecular Sequence Data; Phenylhydrazines; Sequence Homology, Amino Acid | 1995 |
Role of conserved Asn-Tyr-Asp-Tyr sequence in bacterial copper/2,4, 5-trihydroxyphenylalanyl quinone-containing histamine oxidase.
Topics: Amine Oxidase (Copper-Containing); Base Sequence; Conserved Sequence; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Escherichia coli; Kinetics; Molecular Sequence Data; Oxygen Consumption; Phenylhydrazines; Plasmids; Protein Conformation; Spectrophotometry, Atomic | 1996 |
Reactions of the oxidized organic cofactor in copper-depleted bovine serum amine oxidase.
Topics: Amine Oxidase (Copper-Containing); Animals; Benzylamines; Catalysis; Cattle; Copper; Dihydroxyphenylalanine; Enzyme Inhibitors; Fabaceae; Hydrazines; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Phenylhydrazines; Plant Proteins; Plants, Medicinal; Pyridines; Semicarbazides; Species Specificity | 1997 |
The oxidation and reduction reactions of bovine serum amine oxidase. A kinetic study.
Topics: Amine Oxidase (Copper-Containing); Animals; Catalysis; Cattle; Coenzymes; Dihydroxyphenylalanine; Enzyme Inhibitors; Hydrazines; Kinetics; Oxidation-Reduction; Oxygen; Phenylhydrazines | 2000 |
Human kidney diamine oxidase: heterologous expression, purification, and characterization.
Topics: Amine Oxidase (Copper-Containing); Amines; Animals; Binding Sites; Cell Line; Dihydroxyphenylalanine; Drosophila; Humans; Hydrogen-Ion Concentration; Kidney; Kinetics; Molecular Weight; Organ Specificity; Oxidation-Reduction; Phenylhydrazines; Recombinant Proteins | 2002 |
Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases.
Topics: Amine Oxidase (Copper-Containing); Animals; Bacteria; Diamines; Dihydroxyphenylalanine; Drug Design; Enzyme Inhibitors; Mammals; Models, Molecular; Naphthalenes; Phenylhydrazines; Protein Conformation; Protein-Lysine 6-Oxidase; Species Specificity; Time Factors; Titrimetry | 2002 |
Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha.
Topics: Amine Oxidase (Copper-Containing); Binding Sites; Catalysis; Coenzymes; Conserved Sequence; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Ethylamines; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Phenylhydrazines; Pichia; Tyrosine | 2006 |
Characterization of recombinant human diamine oxidase (rhDAO) produced in Chinese Hamster Ovary (CHO) cells.
Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Blotting, Western; CHO Cells; Chromatography, Liquid; Circular Dichroism; Coenzymes; Cricetinae; Cricetulus; Dihydroxyphenylalanine; Electrophoresis, Polyacrylamide Gel; Gene Expression; Glycosylation; Humans; Kinetics; Metals; Peptides; Phenylhydrazines; Polysaccharides; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Substrate Specificity | 2016 |