(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with lithium in 4 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (lithium) | Trials (lithium) | Recent Studies (post-2010) (lithium) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 23,339 | 1,102 | 4,484 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Androutsellis-Theotokis, A; Chen, JG; Huang, CJ; Moczydlowski, E; Ni, YG; Rudnick, G | 1 |
| Kanner, BI; Zhou, Y | 1 |
| Kanner, BI; Shachnai, L; Shimamoto, K | 1 |
| Herz, K; Kozachkov, L; Olkhova, E; Padan, E; Rimon, A | 1 |
4 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and lithium
| Article | Year |
|---|---|
A lithium-induced conformational change in serotonin transporter alters cocaine binding, ion conductance, and reactivity of Cys-109.
Topics: Animals; Carrier Proteins; Cocaine; Cysteine; Glutamates; HeLa Cells; Humans; Lithium; Membrane Glycoproteins; Membrane Potentials; Membrane Transport Proteins; Mesylates; Nerve Tissue Proteins; Protein Conformation; Serotonin Plasma Membrane Transport Proteins; Sodium; Xenopus | 2001 |
Transporter-associated currents in the gamma-aminobutyric acid transporter GAT-1 are conditionally impaired by mutations of a conserved glycine residue.
Topics: Animals; Biotinylation; Conserved Sequence; Cysteine; Electric Conductivity; Female; GABA Plasma Membrane Transport Proteins; gamma-Aminobutyric Acid; Gene Expression; Glycine; HeLa Cells; Humans; Lithium; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Oocytes; Protein Conformation; RNA, Complementary; Sodium; Structure-Activity Relationship; Sulfhydryl Reagents; Transfection; Tritium; Xenopus laevis | 2005 |
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 |