aspartic acid has been researched along with (2-(trimethylammonium)ethyl)methanethiosulfonate in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (20.00) | 18.2507 |
| 2000's | 2 (40.00) | 29.6817 |
| 2010's | 2 (40.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Simpson, MM | 1 |
| Berfield, JL; Chen, N; Reith, ME; Rickey, J | 1 |
| Kanner, BI; Shachnai, L; Shimamoto, K | 1 |
| Herz, K; Kozachkov, L; Olkhova, E; Padan, E; Rimon, A | 1 |
| Qu, S; Rong, X; Zhang, X | 1 |
5 other study(ies) available for aspartic acid and (2-(trimethylammonium)ethyl)methanethiosulfonate
| Article | Year |
|---|---|
Electrostatic and aromatic microdomains within the binding-site crevice of the D2 receptor: contributions of the second membrane-spanning segment.
Topics: Amino Acid Substitution; Aspartic Acid; Binding, Competitive; Cell Line; Cell Membrane; Cysteine; Dopamine Antagonists; Ethyl Methanesulfonate; Humans; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments; Protein Binding; Protein Structure, Tertiary; Receptors, Dopamine D2; Static Electricity; Sulpiride | 1999 |
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation and cocaine binding.
Topics: Alanine; Aspartic Acid; Biological Transport; Biotinylation; Blotting, Western; Cell Line; Cell Membrane; Cocaine; Cystine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Dose-Response Relationship, Drug; Glutamic Acid; Humans; Kinetics; Ligands; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Mutation; Nerve Tissue Proteins; Phenotype; Piperazines; Protein Binding; Protein Conformation; Protein Transport; Sodium; Time Factors; Zinc | 2004 |
Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance.
Topics: Amino Acid Transport System X-AG; Animals; Aspartic Acid; Cell Line; Cloning, Molecular; Cysteine; Dose-Response Relationship, Drug; Drug Interactions; Electric Stimulation; Glutamates; Humans; Ion Channel Gating; Lithium; Membrane Potentials; Mesylates; Microinjections; Mutagenesis; Mutation; Neurons; Oocytes; Patch-Clamp Techniques; Protein Conformation; Protein Structure, Tertiary; Sodium; Sulfhydryl Compounds; Transfection; Xenopus | 2005 |
Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.
Topics: Aspartic Acid; Cations; Cell Membrane; Computer Simulation; Conserved Sequence; Crystallography, X-Ray; Cysteine; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Hydrogen-Ion Concentration; Ion Transport; Lithium; Mesylates; Models, Molecular; Mutation; Periplasm; Phenotype; Protein Conformation; Sodium-Hydrogen Exchangers | 2010 |
A complex relative motion between hairpin loop 2 and transmembrane domain 5 in the glutamate transporter GLT-1.
Topics: Aspartic Acid; Dithiothreitol; Excitatory Amino Acid Transporter 2; Glutamic Acid; HeLa Cells; Humans; Kinetics; Mesylates; Protein Structure, Secondary; Protein Structure, Tertiary; Sodium Chloride; Sulfhydryl Compounds | 2015 |