tyrosine has been researched along with phosphoramidon in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Fournie-Zaluski, MC; Marie-Claire, C; Ruffet, E; Tiraboschi, G | 1 |
| Hatanaka, T; Iwabuchi, M; Yoshiko Uesugi, JA | 1 |
| Devi, LA; Gagnidze, K; Mezei, M; Rozenfeld, R; Zhou, MM | 1 |
3 other study(ies) available for tyrosine and phosphoramidon
| Article | Year |
|---|---|
Differences in transition state stabilization between thermolysin (EC 3.4.24.27) and neprilysin (EC 3.4.24.11).
Topics: Amino Acid Sequence; Aspartic Acid; Bacillus subtilis; Catalytic Domain; Enzyme Stability; Glycopeptides; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Neprilysin; Protease Inhibitors; Protein Conformation; Recombinant Proteins; Thermolysin; Thiorphan; Tyrosine | 1998 |
Purification, characterization cloning, and sequencing of metalloendopeptidase from Streptomyces septatus TH-2.
Topics: Amino Acid Motifs; Amino Acid Sequence; Bacillus; Base Sequence; Binding Sites; Culture Media; Edetic Acid; Electrophoresis, Polyacrylamide Gel; Fluorescence Resonance Energy Transfer; Glucose; Glycopeptides; Hydrogen-Ion Concentration; Kinetics; Metalloendopeptidases; Molecular Sequence Data; Phenylalanine; Polymerase Chain Reaction; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrophotometry, Atomic; Streptomyces; Streptomyces griseus; Substrate Specificity; Temperature; Thermolysin; Tyrosine; Zinc | 2005 |
Homology modeling and site-directed mutagenesis to identify selective inhibitors of endothelin-converting enzyme-2.
Topics: Amino Acid Sequence; Aspartic Acid Endopeptidases; Catalytic Domain; Conserved Sequence; Endothelin-Converting Enzymes; Glycopeptides; Kinetics; Metalloendopeptidases; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Neprilysin; Protein Conformation; Quinolines; Quinoxalines; Recombinant Proteins; Sequence Homology, Amino Acid; Small Molecule Libraries; Structure-Activity Relationship; Tryptophan; Tyrosine | 2008 |