5-androstene-3,17-dione has been researched along with aspartic acid in 3 studies
| Studies (5-androstene-3,17-dione) | Trials (5-androstene-3,17-dione) | Recent Studies (post-2010) (5-androstene-3,17-dione) | Studies (aspartic acid) | Trials (aspartic acid) | Recent Studies (post-2010) (aspartic acid) |
|---|---|---|---|---|---|
| 15 | 0 | 1 | 23,005 | 417 | 4,018 |
| Protein | Taxonomy | 5-androstene-3,17-dione (IC50) | aspartic acid (IC50) |
|---|---|---|---|
| Glutamate receptor ionotropic, NMDA 1 | Rattus norvegicus (Norway rat) | 1.638 | |
| Excitatory amino acid transporter 1 | Homo sapiens (human) | 90.1265 | |
| Excitatory amino acid transporter 2 | Homo sapiens (human) | 11 | |
| Glutamate receptor ionotropic, NMDA 2A | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 2B | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 2C | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 2D | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 3B | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 3A | Rattus norvegicus (Norway rat) | 1.638 |
| 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 |
|---|---|
| Benisek, WF; Holman, CM | 1 |
| Cha, SS; Choi, KY; Hong, BH; Lee, HS; Nam, GH; Oh, YH; Yun, YS | 1 |
| Kubli-Garfias, C; Sharma, K; Vázquez-Ramírez, R | 1 |
3 other study(ies) available for 5-androstene-3,17-dione and aspartic acid
| Article | Year |
|---|---|
Insights into the catalytic mechanism and active-site environment of Comamonas testosteroni delta 5-3-ketosteroid isomerase as revealed by site-directed mutagenesis of the catalytic base aspartate-38.
Topics: Androstenedione; Aspartic Acid; Binding Sites; Catalysis; Cloning, Molecular; Escherichia coli; Gram-Negative Aerobic Bacteria; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Spectrophotometry, Ultraviolet; Steroid Isomerases; Substrate Specificity | 1995 |
The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.
Topics: Androstenedione; Aspartic Acid; Binding Sites; Catalysis; Catalytic Domain; Comamonas testosteroni; Conserved Sequence; Crystallography, X-Ray; Enzyme Stability; Equilenin; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutation; Proline; Protein Binding; Protein Folding; Protein Structure, Tertiary; Steroid Isomerases; Structure-Activity Relationship; Substrate Specificity; Thermodynamics | 2003 |
A theoretical model of the catalytic mechanism of the Delta5-3-ketosteroid isomerase reaction.
Topics: Androstenedione; Aspartic Acid; Catalysis; Models, Chemical; Models, Molecular; Stereoisomerism; Steroid Isomerases; Tyrosine | 2006 |