aspartic acid has been researched along with fulvestrant in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 1 (33.33) | 2.80 |
| Authors | Studies |
|---|---|
| Bentrem, DJ; Jordan, VC; Liu, H; MacGregor Schafer, J; Zapf, JW | 1 |
| Jordan, VC; Liu, H; Pearce, ST | 1 |
| Bach, C; Baumert, TF; Brino, L; Crouchet, E; El Saghire, H; Garcia, T; Heydmann, L; Kopp, A; Pale, P; Pessaux, P; Schuster, C; Sureau, C; Turon-Lagot, V; Verrier, ER; Weiss, A; Zeisel, MB | 1 |
3 other study(ies) available for aspartic acid and fulvestrant
| Article | Year |
|---|---|
Allosteric silencing of activating function 1 in the 4-hydroxytamoxifen estrogen receptor complex is induced by substituting glycine for aspartate at amino acid 351.
Topics: Allosteric Regulation; Amino Acid Substitution; Aspartic Acid; Binding Sites; Drug Interactions; Estradiol; Estrogen Receptor Modulators; Fulvestrant; Glycine; Humans; Kinetics; Ligands; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Tertiary; Raloxifene Hydrochloride; Receptors, Estrogen; RNA, Messenger; Tamoxifen; Transfection; Transforming Growth Factor alpha; Tumor Cells, Cultured | 2000 |
Modulation of estrogen receptor alpha function and stability by tamoxifen and a critical amino acid (Asp-538) in helix 12.
Topics: Aspartic Acid; Blotting, Northern; Blotting, Western; Cell Line; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Endoplasmic Reticulum; Estradiol; Estrogen Antagonists; Estrogen Receptor alpha; Fulvestrant; Humans; Ligands; Luciferases; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Estrogen; RNA, Messenger; Tamoxifen; Time Factors; Transcription, Genetic; Transfection; Transforming Growth Factor alpha; Tumor Cells, Cultured | 2003 |
Combined small molecule and loss-of-function screen uncovers estrogen receptor alpha and CAD as host factors for HDV infection and antiviral targets.
Topics: Antiviral Agents; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Cell Line; Dihydroorotase; Estrogen Receptor alpha; Estrogen Receptor Antagonists; Fulvestrant; Gene Silencing; Hepatitis D, Chronic; Hepatitis Delta Virus; Hepatocytes; Humans; Hypoxia-Inducible Factor 1, alpha Subunit; Insulin Resistance; Life Cycle Stages; Loss of Function Mutation; Phosphonoacetic Acid; Pyrimidines; RNA Interference; RNA, Small Interfering; RNA, Viral; Signal Transduction; Virus Replication | 2020 |