(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with serine in 4 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (serine) | Trials (serine) | Recent Studies (post-2010) (serine) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 23,914 | 115 | 6,084 |
| Protein | Taxonomy | (2-(trimethylammonium)ethyl)methanethiosulfonate (IC50) | serine (IC50) |
|---|---|---|---|
| Acetylcholinesterase | Electrophorus electricus (electric eel) | 0.015 | |
| Cholinesterase | Equus caballus (horse) | 0.016 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Biber, J; Forster, IC; Lambert, G; Murer, H | 1 |
| Cui, Y; Fan, Z; Wang, W | 1 |
| Björquist, A; Hallén, S; Ostlund-Lindqvist, AM; Sachs, G | 1 |
| Ding, XQ; Dolu, V; Hadac, EM; Miller, LJ; Schuetz, M | 1 |
4 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and serine
| Article | Year |
|---|---|
Cysteine residues and the structure of the rat renal proximal tubular type II sodium phosphate cotransporter (rat NaPi IIa).
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cysteine; Disulfides; Ethyl Methanesulfonate; Kidney Tubules, Proximal; Mesylates; Methyl Methanesulfonate; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Tertiary; Rats; Reducing Agents; Serine; Sodium-Phosphate Cotransporter Proteins; Sodium-Phosphate Cotransporter Proteins, Type II; Sodium-Phosphate Cotransporter Proteins, Type IIa; Symporters; Xenopus laevis | 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 |
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 |
Disulfide bond structure and accessibility of cysteines in the ectodomain of the cholecystokinin receptor: specific mono-reactive receptor constructs examine charge-sensitivity of loop regions.
Topics: Animals; CHO Cells; Cricetinae; Cricetulus; Cysteine; Disulfides; Mesylates; Mutation; Receptors, Cholecystokinin; Serine; Sulfhydryl Reagents | 2003 |