D-tryptophan has been researched along with tryptophan in 22 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (4.55) | 18.2507 |
| 2000's | 11 (50.00) | 29.6817 |
| 2010's | 8 (36.36) | 24.3611 |
| 2020's | 2 (9.09) | 2.80 |
| Authors | Studies |
|---|---|
| Hupe, D; Hupe, L; Johnson, LL; Nordan, I; Ye, QZ | 1 |
| Cha, SH; Chairoungdua, A; Endou, H; Kanai, Y; Kim, DK; Matsuo, H | 1 |
| Parkkila, AK; Parkkila, S; Puccetti, L; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
| 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 |
| Innocenti, A; Scozzafava, A; Supuran, CT; Temperini, C | 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 |
| 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 |
| DeRose, EF; Duff, MR; Gabel, SA; Howell, EE; Krahn, JM; London, RE; Pedersen, LC | 1 |
| Blain, JM; Gorman, JL; Goshu, GM; Grote, DL; Hagen, TJ; Hofstetter, H; Horn, JR; Muller, C; Ranieri, G; Walter, RL; Watkins, SM | 1 |
22 other study(ies) available for D-tryptophan and tryptophan
| Article | Year |
|---|---|
A recombinant human stromelysin catalytic domain identifying tryptophan derivatives as human stromelysin inhibitors.
Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Catalysis; Escherichia coli; Humans; Matrix Metalloproteinase 3; Metalloendopeptidases; Molecular Sequence Data; Peptide Fragments; Recombinant Proteins; Tryptophan | 1994 |
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 isozyme XIII with amino acids and amines.
Topics: Amines; Amino Acids; Carbonic Anhydrases; Enzyme Activators; Isoenzymes | 2006 |
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: kinetic and X-ray crystallographic study for the interaction of D- and L-tryptophan with the mammalian isoforms I-XIV.
Topics: Carbonic Anhydrases; Catalytic Domain; Crystallography, X-Ray; Enzyme Activators; Epinephrine; Histamine; Kinetics; Phenylalanine; Protein Conformation; Protein Isoforms; Stereoisomerism; Tryptophan | 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 |
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 |
The Structural Basis for Nonsteroidal Anti-Inflammatory Drug Inhibition of Human Dihydrofolate Reductase.
Topics: Anti-Inflammatory Agents, Non-Steroidal; Binding Sites; Crystallography, X-Ray; Drug Design; Folic Acid; Folic Acid Antagonists; Humans; Models, Molecular; Tetrahydrofolate Dehydrogenase | 2020 |
Structural and biophysical characterization of the Burkholderia pseudomallei IspF inhibitor L-tryptophan hydroxamate.
Topics: Bacterial Proteins; Binding Sites; Burkholderia pseudomallei; Dose-Response Relationship, Drug; Enzyme Inhibitors; Models, Molecular; Molecular Structure; Structure-Activity Relationship; Tryptophan | 2021 |