(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with valine in 3 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (valine) | Trials (valine) | Recent Studies (post-2010) (valine) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 15,465 | 1,176 | 3,932 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Freedman, ND; Grant, M; Hawrot, E; McLaughlin, JT; Russin, TS; Spura, A | 1 |
| Björquist, A; Hallén, S; Ostlund-Lindqvist, AM; Sachs, G | 1 |
| Pajor, AM; Randolph, KM | 1 |
3 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and valine
| Article | Year |
|---|---|
Probing the agonist domain of the nicotinic acetylcholine receptor by cysteine scanning mutagenesis reveals residues in proximity to the alpha-bungarotoxin binding site.
Topics: Acetylcholine; Animals; Bungarotoxins; Cysteine; Humans; Indicators and Reagents; Mesylates; Mice; Mutagenesis, Site-Directed; Nicotinic Agonists; Nicotinic Antagonists; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Protein Binding; Receptors, Nicotinic; Torpedo; Tryptophan; Valine | 1999 |
Identification of a region of the ileal-type sodium/bile acid cotransporter interacting with a competitive bile acid transport inhibitor.
Topics: Amino Acid Sequence; Animals; Bile Acids and Salts; Binding, Competitive; Biological Transport, Active; Carrier Proteins; Cell Line; CHO Cells; Cricetinae; Cysteine; Humans; Hydroxysteroid Dehydrogenases; Ileum; Kinetics; Membrane Glycoproteins; Mesylates; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Organic Anion Transporters, Sodium-Dependent; Peptide Fragments; Rats; Recombinant Fusion Proteins; Sequence Alignment; Serine; Symporters; Taurocholic Acid; Thiazepines; Threonine; Valine | 2002 |
Conformationally sensitive residues in extracellular loop 5 of the Na+/dicarboxylate co-transporter.
Topics: Amino Acid Sequence; Animals; Anions; Biological Transport; Biotinylation; Blotting, Western; Cations; Cell Line; Cell Membrane; Cloning, Molecular; Cysteine; Cystine; Dicarboxylic Acid Transporters; Dose-Response Relationship, Drug; Humans; Indicators and Reagents; Inhibitory Concentration 50; Ions; Kinetics; Mesylates; Models, Chemical; Molecular Sequence Data; Mutagenesis; Mutation; Organic Anion Transporters, Sodium-Dependent; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits; Sequence Homology, Amino Acid; Sodium; Symporters; Temperature; Threonine; Time Factors; Valine | 2005 |