Compounds > (2-(trimethylammonium)ethyl)methanethiosulfonate
Page last updated: 2024-09-02

(2-(trimethylammonium)ethyl)methanethiosulfonate and taurine

(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with taurine in 3 studies

Compound Research Comparison

Studies
((2-(trimethylammonium)ethyl)methanethiosulfonate)		Trials
((2-(trimethylammonium)ethyl)methanethiosulfonate)		Recent Studies (post-2010)
((2-(trimethylammonium)ethyl)methanethiosulfonate)		Studies
(taurine)		Trials
(taurine)		Recent Studies (post-2010) (taurine)
14301710,3014302,438

Protein Interaction Comparison

ProteinTaxonomy(2-(trimethylammonium)ethyl)methanethiosulfonate (IC50)taurine (IC50)
Sodium- and chloride-dependent taurine transporterHomo sapiens (human)10

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Haddrill, JL; Han, NL; Lynch, JW1
Absalom, NL; Kaplan, W; Lewis, TM; Pierce, KD; Schofield, PR1
Clements, JD; Han, NL; Lynch, JW1

Other Studies

3 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and taurine

ArticleYear
Characterization of a glycine receptor domain that controls the binding and gating mechanisms of the beta-amino acid agonist, taurine.
    Journal of neurochemistry, 2001, Volume: 79, Issue:3

    Topics: Amino Acid Substitution; Binding Sites; Cell Line; Cysteine; Glycine; Humans; Ion Channel Gating; Kidney; Mesylates; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Receptors, Glycine; Sulfhydryl Reagents; Taurine

2001
Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.
    The Journal of biological chemistry, 2003, Dec-12, Volume: 278, Issue:50

    Topics: Acetylcholine; Amino Acid Sequence; Carrier Proteins; Cysteine; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; Glycine; Humans; Indicators and Reagents; Ions; Ligands; Lysine; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Glycine; Sequence Homology, Amino Acid; Taurine; Time Factors

2003
Comparison of taurine- and glycine-induced conformational changes in the M2-M3 domain of the glycine receptor.
    The Journal of biological chemistry, 2004, May-07, Volume: 279, Issue:19

    Topics: Arginine; Binding Sites; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; Glycine; Humans; Inhibitory Concentration 50; Kinetics; Lysine; Mesylates; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Structure, Tertiary; Receptors, Glycine; Sulfhydryl Reagents; Taurine; Time Factors

2004