aspartic acid has been researched along with cgp 12177 in 2 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Ballesteros, JA; Gether, U; Javitch, JA; Jensen, AD; Liapakis, G; Rasmussen, SG; Shi, L | 1 |
Colledge, WH; Joseph, SS; Kaumann, AJ | 1 |
2 other study(ies) available for aspartic acid and cgp 12177
Article | Year |
---|---|
Activation of the beta 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6.
Topics: Adrenergic beta-Agonists; Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Aspartic Acid; Cell Line; Cell Membrane; Chlorocebus aethiops; Conserved Sequence; COS Cells; Cyclic AMP; Cytoplasm; Glutamic Acid; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Propanolamines; Protein Structure, Secondary; Receptors, Adrenergic, beta-2; Recombinant Proteins; Transfection | 2001 |
Aspartate138 is required for the high-affinity ligand binding site but not for the low-affinity binding site of the beta1-adrenoceptor.
Topics: Adrenergic beta-Agonists; Adrenergic beta-Antagonists; Animals; Aspartic Acid; Binding Sites; Bupranolol; CHO Cells; Cricetinae; Cricetulus; Drug Interactions; Isoproterenol; Ligands; Propanolamines; Receptors, Adrenergic, beta-1 | 2004 |