(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with isoleucine in 4 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (isoleucine) | Trials (isoleucine) | Recent Studies (post-2010) (isoleucine) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 5,938 | 74 | 1,138 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chen, JG; Rudnick, G; Sachpatzidis, A | 1 |
| Chen, JG; Rudnick, G | 1 |
| Cui, Y; Fan, Z; Wang, W | 1 |
| Bartlett, MC; Clarke, DM; Loo, TW | 1 |
4 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and isoleucine
| Article | Year |
|---|---|
The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding.
Topics: Asparagine; Binding Sites; Carrier Proteins; Cell Line; Cell Membrane; Cocaine; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Isoleucine; Ligands; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Structure, Secondary; Serotonin; Serotonin Plasma Membrane Transport Proteins; Structure-Activity Relationship; Tyrosine | 1997 |
Permeation and gating residues in serotonin transporter.
Topics: Allosteric Regulation; Amino Acid Substitution; Carrier Proteins; Chlorides; Cocaine; Humans; Hydrogen; Ion Channel Gating; Ion Transport; Isoleucine; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Norepinephrine Plasma Membrane Transport Proteins; Oxidation-Reduction; Potassium; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Recombinant Fusion Proteins; Reducing Agents; Serotonin; Serotonin Plasma Membrane Transport Proteins; Sodium; Sulfhydryl Compounds; Symporters | 2000 |
Cytoplasmic vestibule of the weak inward rectifier Kir6.2 potassium channel.
Topics: Adenosine Triphosphate; Animals; Cells, Cultured; COS Cells; Cysteine; Cytoplasm; DNA, Complementary; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Immunohistochemistry; Isoleucine; Mesylates; Models, Biological; Models, Chemical; Mutagenesis, Site-Directed; Naphthalenesulfonates; Patch-Clamp Techniques; Potassium; Potassium Channels, Inwardly Rectifying; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Recombinant Fusion Proteins; Serine; Spermine; Sulfhydryl Reagents; Transfection | 2002 |
The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding Sites; Biological Transport; Buffers; Cell Line; Colchicine; Cyclosporine; Cysteine; Drug Resistance, Multiple; Gene Expression Regulation; Humans; Hydrolysis; Isoleucine; Mesylates; Mutation; Rhodamines; Verapamil; Water | 2004 |