D-tryptophan has been researched along with D-tyrosine in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (14.29) | 29.6817 |
2010's | 6 (85.71) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cha, SH; Chairoungdua, A; Endou, H; Kanai, Y; Kim, DK; Matsuo, H | 1 |
Innocenti, A; Leewattanapasuk, W; Manole, G; Mühlschlegel, FA; Scozzafava, A; Supuran, CT | 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 |
Anthony, A; Augustyn, E; Bauer, J; Campbell, J; Chien, HC; Colas, C; Finke, K; Flint, A; Fotiadis, D; Giacomini, KM; Hall, C; Hansen, L; Heeren, N; Hernandez, C; Schlessinger, A; Springer, S; Stoner, L; Thomas, AA; Venteicher, B; Zur, AA | 1 |
7 other study(ies) available for D-tryptophan and D-tyrosine
Article | Year |
---|---|
Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters.
Topics: Amino Acid Sequence; Amino Acid Transport Systems; Amino Acid Transport Systems, Neutral; Animals; Anion Transport Proteins; Bacterial Proteins; Carrier Proteins; Cloning, Molecular; Escherichia coli Proteins; Female; Intestine, Small; Kinetics; Levodopa; Mice; Molecular Sequence Data; Oocytes; Phenylalanine; Rats; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity; Tryptophan; Tyrosine; Xenopus laevis | 2001 |
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 |
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 |
Reevaluating the Substrate Specificity of the L-Type Amino Acid Transporter (LAT1).
Topics: Amino Acid Transport Systems; Antiporters; Escherichia coli Proteins; HEK293 Cells; Humans; Large Neutral Amino Acid-Transporter 1; Ligands; Molecular Docking Simulation; Phenylalanine; Stereoisomerism; Structural Homology, Protein; Structure-Activity Relationship; Substrate Specificity | 2018 |