aspartic acid has been researched along with (2-sulfonatoethyl)methanethiosulfonate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Simpson, MM | 1 |
| Ennis, IL; Li, RA; Marbán, E; Tomaselli, GF; Vélez, P | 1 |
| Haska, CL; Hou, Z; Matherly, LH; Stapels, SE | 1 |
| Herz, K; Kozachkov, L; Olkhova, E; Padan, E; Rimon, A | 1 |
4 other study(ies) available for aspartic acid and (2-sulfonatoethyl)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 |
Novel structural determinants of mu-conotoxin (GIIIB) block in rat skeletal muscle (mu1) Na+ channels.
Topics: Amino Acid Substitution; Animals; Aspartic Acid; Binding Sites; Cell Line; Conotoxins; Ethyl Methanesulfonate; Glutamic Acid; Humans; Kinetics; Mesylates; Models, Molecular; Muscle, Skeletal; Mutagenesis, Site-Directed; Protein Structure, Secondary; Rats; Sodium Channel Blockers; Sodium Channels; Transfection | 2000 |
Localization of a substrate binding domain of the human reduced folate carrier to transmembrane domain 11 by radioaffinity labeling and cysteine-substituted accessibility methods.
Topics: Amino Acid Sequence; Anions; Aspartic Acid; Blotting, Western; Cell Line; Cell Membrane; Cysteine; Cytosol; Folic Acid; Glutamine; HeLa Cells; Histidine; Humans; K562 Cells; Leucovorin; Membrane Transport Proteins; Mesylates; Microscopy, Fluorescence; Molecular Sequence Data; Mutagenesis; Mutation; Peptides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Reduced Folate Carrier Protein; Sulfhydryl Reagents; Temperature; Thiocyanates; Time Factors; Transfection; Tyrosine | 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 |