4-aminophenylalanine has been researched along with tyrosine in 20 studies
| Studies (4-aminophenylalanine) | Trials (4-aminophenylalanine) | Recent Studies (post-2010) (4-aminophenylalanine) | Studies (tyrosine) | Trials (tyrosine) | Recent Studies (post-2010) (tyrosine) |
|---|---|---|---|---|---|
| 52 | 0 | 14 | 44,273 | 846 | 8,225 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (10.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 10 (50.00) | 29.6817 |
| 2010's | 8 (40.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Innocenti, A; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Innocenti, A; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Innocenti, A; Kaila, K; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Nishimori, I; Pastorek, J; Pastorekova, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Ferry, JG; Innocenti, A; Scozzafava, A; Supuran, CT; Zimmerman, SA | 1 |
| Arslan, O; Aydin, M; Guler, OO; Innocenti, A; Isik, S; Kockar, F; Scozzafava, A; Supuran, CT | 1 |
| Hilvo, M; Innocenti, A; Parkkila, S; Scozzafava, A; Supuran, CT | 1 |
| Hall, RA; Innocenti, A; Mühlschlegel, FA; Scozzafava, A; Supuran, CT | 1 |
| Innocenti, A; Leewattanapasuk, W; Manole, G; Mühlschlegel, FA; Scozzafava, A; Supuran, CT | 1 |
| Bertucci, A; Supuran, CT; Tambutté, S; Vullo, D; Zoccola, D | 1 |
| Capasso, C; Carginale, V; De Luca, V; Rossi, M; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Akdemir, A; Capasso, C; Carginale, V; De Luca, V; Rossi, M; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| Capasso, C; Del Prete, S; Supuran, CT; Vullo, D | 1 |
| AlOthman, Z; Capasso, C; Del Prete, S; Donald, WA; Osman, SM; Supuran, CT; Vullo, D | 1 |
| Francis, MM; Jones, A; Vining, LC | 1 |
| Beschle, HG; Lingens, F; Süssmuth, R | 1 |
| Chang, MC; Nocera, DG; Stubbe, J; Yee, CS | 1 |
| Hohsaka, T; Kajihara, D; Sisido, M | 1 |
| Poulter, CD; Rudolf, JD | 1 |
20 other study(ies) available for 4-aminophenylalanine and tyrosine
| Article | Year |
|---|---|
Carbonic anhydrase activators: an activation study of the human mitochondrial isoforms VA and VB with amino acids and amines.
Topics: Amines; Amino Acids; Carbonic Anhydrases; Catalysis; Enzyme Activation; Humans; Kinetics; Mitochondrial Proteins; Protein Isoforms; Structure-Activity Relationship | 2007 |
Carbonic anhydrase activators: the first activation study of the human secretory isoform VI with amino acids and amines.
Topics: Amines; Amino Acid Sequence; Amino Acids; Carbonic Anhydrases; Cloning, Molecular; Enzyme Activation; Gene Expression Regulation, Enzymologic; Humans; Molecular Sequence Data; Protein Isoforms; Protein Subunits | 2007 |
Carbonic anhydrase activators: activation of the human isoforms VII (cytosolic) and XIV (transmembrane) with amino acids and amines.
Topics: Amines; Amino Acid Sequence; Amino Acids; Carbonic Anhydrases; Enzyme Activation; Enzyme Activators; Humans; Isoenzymes; Molecular Sequence Data; Sequence Homology, Amino Acid | 2007 |
Carbonic anhydrase activators: activation of the human tumor-associated isozymes IX and XII with amino acids and amines.
Topics: Amines; Amino Acids; Antigens, Neoplasm; Carbonic Anhydrase IX; Carbonic Anhydrases; Conserved Sequence; Enzyme Activation; Humans; Isoenzymes; Kinetics; Molecular Sequence Data; Molecular Structure; Neoplasms; Sequence Alignment; Structure-Activity Relationship | 2008 |
Carbonic anhydrase activators: Activation of the human cytosolic isozyme III and membrane-associated isoform IV with amino acids and amines.
Topics: Amines; Amino Acids; Binding Sites; Carbonic Anhydrase III; Carbonic Anhydrase IV; Cell Membrane; Cytosol; Enzyme Activation; Histidine; Humans; Isoenzymes; Molecular Structure; Morpholines; Serotonin; Stereoisomerism | 2008 |
Carbonic anhydrase activators: activation of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases with amino acids and amines.
Topics: Amines; Amino Acids; Archaea; Carbonic Anhydrases; Catalysis; Molecular Structure; Phenylalanine; Stereoisomerism; Tyrosine | 2008 |
Carbonic anhydrase activators: activation of the beta-carbonic anhydrase Nce103 from the yeast Saccharomyces cerevisiae with amines and amino acids.
Topics: Amino Acids; Candida albicans; Carbonic Anhydrases; Catalysis; Catalytic Domain; Cryptococcus neoformans; Drug Design; Enzyme Activation; Epinephrine; Humans; Kinetics; Models, Chemical; Protein Isoforms; Saccharomyces cerevisiae; Tryptophan | 2009 |
Carbonic anhydrase activators. Activation of the membrane-associated isoform XV with amino acids and amines.
Topics: Amines; Amino Acid Sequence; Amino Acids; Animals; Carbonic Anhydrases; Enzyme Activators; Humans; Kinetics; Mice; Molecular Sequence Data; Protein Isoforms; Recombinant Proteins; Sequence Homology, Amino Acid; Structure-Activity Relationship | 2009 |
Carbonic anhydrase activators: activation of the beta-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids.
Topics: Amines; Amino Acids; Candida albicans; Carbonic Anhydrase I; Carbonic Anhydrases; Cryptococcus neoformans; Enzyme Activation; Structure-Activity Relationship | 2010 |
Carbonic anhydrase activators: Activation of the beta-carbonic anhydrase from the pathogenic yeast Candida glabrata with amines and amino acids.
Topics: Amines; Amino Acids; Candida glabrata; Carbonic Anhydrases; Catalytic Domain; Enzyme Activation; Humans; Kinetics; Models, Molecular; Recombinant Proteins; Structure-Activity Relationship | 2010 |
Carbonic anhydrase activators. The first activation study of a coral secretory isoform with amino acids and amines.
Topics: Amines; Amino Acids; Animals; Anthozoa; Carbonic Anhydrases; Enzyme Activation; Humans; Isoenzymes; Kinetics; Molecular Structure; Stereoisomerism; Structure-Activity Relationship | 2010 |
The first activation study of a bacterial carbonic anhydrase (CA). The thermostable α-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines.
Topics: Amines; Amino Acids; Carbon Dioxide; Carbonic Anhydrases; Enzyme Activation; Gram-Negative Chemolithotrophic Bacteria; Kinetics | 2012 |
The extremo-α-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines.
Topics: Amines; Amino Acids; Bacteria; Carbonic Anhydrases; Catalysis; Structure-Activity Relationship; Sulfur Compounds | 2013 |
Carbonic anhydrase activators: Activation of the β-carbonic anhydrase from Malassezia globosa with amines and amino acids.
Topics: Amines; Amino Acids; Antifungal Agents; Carbonic Anhydrases; Dandruff; Dose-Response Relationship, Drug; Ligands; Malassezia; Molecular Structure; Structure-Activity Relationship | 2016 |
Burkholderia pseudomallei γ-carbonic anhydrase is strongly activated by amino acids and amines.
Topics: Amines; Amino Acids; Burkholderia pseudomallei; Carbonic Anhydrases; Dose-Response Relationship, Drug; Humans; Molecular Structure; Structure-Activity Relationship | 2017 |
Biosynthesis of chloramphenicol in Streptomyces sp. 3022a. Properties of an aminotransferase accepting p-aminophenylalanine as a substrate.
Topics: Amino Acids, Diamino; Cell-Free System; Chloramphenicol; Phenylalanine; Stereoisomerism; Streptomyces; Substrate Specificity; Transaminases; Tyrosine | 1978 |
Conversion of chloramphenicol degradation products by tyrosine aminotransferase from Flavobacteria.
Topics: Chloramphenicol; Flavobacterium; Kinetics; Phenylalanine; Substrate Specificity; Tyrosine; Tyrosine Transaminase | 1982 |
Site-specific replacement of a conserved tyrosine in ribonucleotide reductase with an aniline amino acid: a mechanistic probe for a redox-active tyrosine.
Topics: Hydrogen Bonding; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Protons; Ribonucleotide Reductases; Tyrosine | 2004 |
Synthesis and sequence optimization of GFP mutants containing aromatic non-natural amino acids at the Tyr66 position.
Topics: Cell-Free System; Codon; Escherichia coli; Gene Library; Green Fluorescent Proteins; Mutagenesis; Mutation; Phenylalanine; Protein Engineering; RNA, Transfer; Tyrosine | 2005 |
Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives.
Topics: Dimethylallyltranstransferase; Escherichia coli; Fungal Proteins; Gene Expression; Hemiterpenes; Kinetics; Organophosphorus Compounds; Phenylalanine; Piperazines; Prenylation; Recombinant Proteins; Saccharomycetales; Substrate Specificity; Sulfhydryl Compounds; Tryptophan; Tyrosine | 2013 |