(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with tryptophan in 3 studies
Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (tryptophan) | Trials (tryptophan) | Recent Studies (post-2010) (tryptophan) |
---|---|---|---|---|---|
143 | 0 | 17 | 32,762 | 936 | 7,183 |
Protein | Taxonomy | (2-(trimethylammonium)ethyl)methanethiosulfonate (IC50) | tryptophan (IC50) |
---|---|---|---|
Myeloperoxidase | Homo sapiens (human) | 2.25 |
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 |
Carbonneau, E; Chahine, M; Vijayaragavan, K | 1 |
Das, S; Gether, U; Goldberg, N; Javitch, JA; Kniazeff, J; Loland, CJ; Quick, M; Sitte, HH | 1 |
3 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and tryptophan
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 |
A tryptophan residue (W736) in the amino-terminus of the P-segment of domain II is involved in pore formation in Na(v)1.4 voltage-gated sodium channels.
Topics: Amino Acid Sequence; Animals; Cadmium; Conotoxins; Electric Conductivity; Female; Ions; Mesylates; Muscle Proteins; Mutation; Oocytes; Protein Subunits; Rats; Sodium Channels; Sulfhydryl Reagents; Tetrodotoxin; Tryptophan; Xenopus laevis | 2002 |
Intramolecular cross-linking in a bacterial homolog of mammalian SLC6 neurotransmitter transporters suggests an evolutionary conserved role of transmembrane segments 7 and 8.
Topics: Animals; Biological Evolution; Cross-Linking Reagents; Dose-Response Relationship, Drug; Escherichia coli; Extracellular Space; Gene Expression; Mammals; Membrane Transport Proteins; Mercury; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Protein Binding; Protein Structure, Quaternary; Sequence Homology, Amino Acid; Structure-Activity Relationship; Tritium; Tryptophan | 2005 |