glutamate thiol has been researched along with organophosphonates in 4 studies
| Studies (glutamate thiol) | Trials (glutamate thiol) | Recent Studies (post-2010) (glutamate thiol) | Studies (organophosphonates) | Trials (organophosphonates) | Recent Studies (post-2010) (organophosphonates) |
|---|---|---|---|---|---|
| 7 | 0 | 0 | 9,968 | 880 | 3,596 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Corvol, P; Iturrioz, X; Llorens-Cortès, C; Vazeux, G | 1 |
| Célérier, J; Corvol, P; Iturrioz, X; Llorens-Cortès, C; Vazeux, G | 1 |
| Iturrioz, X; Llorens-Cortes, C; Maigret, B; Okada, M; Rozenfeld, R | 1 |
| Claperon, C; Inguimbert, N; Iturrioz, X; Llorens-Cortes, C; Maigret, B; Okada, M; Roques, B; Rozenfeld, R | 1 |
4 other study(ies) available for glutamate thiol and organophosphonates
| Article | Year |
|---|---|
A tyrosine residue essential for catalytic activity in aminopeptidase A.
Topics: Amino Acid Substitution; Aminopeptidases; Animals; Binding Sites; COS Cells; Enzyme Inhibitors; Glutamates; Glutamyl Aminopeptidase; Histidine; Imidazoles; Kinetics; Metalloendopeptidases; Mutagenesis, Site-Directed; Organophosphonates; Phenylalanine; Recombinant Proteins; Tyrosine | 1997 |
Histidine 450 plays a critical role in catalysis and, with Ca2+, contributes to the substrate specificity of aminopeptidase A.
Topics: Amino Acid Sequence; Aminopeptidases; Animals; Asparagine; Calcium; Catalysis; CHO Cells; Cricetinae; Dose-Response Relationship, Drug; Enzyme Activation; Enzyme Inhibitors; Glutamates; Glutamyl Aminopeptidase; Histidine; Humans; Lysine; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Organophosphonates; Rats; Recombinant Proteins; Substrate Specificity; Sulfhydryl Compounds | 2000 |
Contribution of molecular modeling and site-directed mutagenesis to the identification of a new residue, glutamate 215, involved in the exopeptidase specificity of aminopeptidase A.
Topics: Amino Acid Sequence; Animals; CHO Cells; Cricetinae; Enzyme Activation; Exopeptidases; Glutamates; Glutamic Acid; Glutamyl Aminopeptidase; Histidine; Mice; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Organophosphonates; Protein Structure, Tertiary; Recombinant Proteins; Sequence Alignment; Substrate Specificity; Transfection | 2003 |
Asp218 participates with Asp213 to bind a Ca2+ atom into the S1 subsite of aminopeptidase A: a key element for substrate specificity.
Topics: Amino Acid Sequence; Amino Acids; Animals; Aspartic Acid; Binding Sites; Calcium; CHO Cells; Cricetinae; Cricetulus; Enzyme Inhibitors; Glutamates; Glutamyl Aminopeptidase; Kinetics; Mice; Models, Molecular; Mutagenesis, Site-Directed; Organophosphonates; Substrate Specificity; Sulfhydryl Compounds | 2008 |