Page last updated: 2024-09-02

(2-(trimethylammonium)ethyl)methanethiosulfonate and methanethiosulfonate

(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with methanethiosulfonate in 4 studies

Compound Research Comparison

Studies
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Trials
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Recent Studies (post-2010)
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Studies
(methanethiosulfonate)
Trials
(methanethiosulfonate)
Recent Studies (post-2010) (methanethiosulfonate)
143017153045

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (25.00)18.2507
2000's3 (75.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Kriegler, S; Sudweeks, S; Yakel, JL1
Liu, J; Siegelbaum, SA1
Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR1
Christie, DL; Dodd, JR1

Other Studies

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

ArticleYear
The nicotinic alpha4 receptor subunit contributes to the lining of the ion channel pore when expressed with the 5-HT3 receptor subunit.
    The Journal of biological chemistry, 1999, Feb-12, Volume: 274, Issue:7

    Topics: Animals; Cysteine; Genetic Engineering; Indicators and Reagents; Mesylates; Oocytes; Receptors, Nicotinic; Receptors, Serotonin; Receptors, Serotonin, 5-HT3; Silver Nitrate; Xenopus

1999
Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels.
    Neuron, 2000, Volume: 28, Issue:3

    Topics: Animals; Bacterial Proteins; Cattle; Cells, Cultured; Cyclic Nucleotide-Gated Cation Channels; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channel Gating; Ion Channels; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Potassium Channels; Protein Conformation; Protein Structure, Secondary; Retinal Rod Photoreceptor Cells; Sequence Homology, Amino Acid; Sulfhydryl Reagents; Water; Xenopus

2000
CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.
    The Journal of general physiology, 2001, Volume: 118, Issue:4

    Topics: Animals; Anions; Arginine; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Disulfides; Electric Conductivity; Ethyl Methanesulfonate; Female; Humans; Hydrogen-Ion Concentration; Lysine; Membrane Potentials; Mercaptoethanol; Mesylates; Models, Biological; Oocytes; Patch-Clamp Techniques; Perfusion; Xenopus

2001
Substituted cysteine accessibility of the third transmembrane domain of the creatine transporter: defining a transport pathway.
    The Journal of biological chemistry, 2005, Sep-23, Volume: 280, Issue:38

    Topics: Amino Acid Sequence; Binding Sites; Biological Transport; Biotinylation; Cell Line; Cell Membrane; Chlorine; Creatine; Cysteine; Dose-Response Relationship, Drug; Humans; Ions; Membrane Transport Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis; Mutation; Protein Binding; Protein Structure, Tertiary; Sodium; Solvents; Sulfhydryl Reagents; Time Factors; Transfection

2005