Page last updated: 2024-09-02

(2-(trimethylammonium)ethyl)methanethiosulfonate and chlorine

(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with chlorine in 5 studies

Compound Research Comparison

Studies
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Trials
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Recent Studies (post-2010)
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Studies
(chlorine)
Trials
(chlorine)
Recent Studies (post-2010) (chlorine)
14301745,6895717,225
14301711,761963,150

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (60.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chen, JG; Rudnick, G1
Bai, Y; Hwang, TC; Li, M1
Blount, P; Yang, LM1
Kanner, BI; Zomot, E1
Christie, DL; Dodd, JR1

Other Studies

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

ArticleYear
Permeation and gating residues in serotonin transporter.
    Proceedings of the National Academy of Sciences of the United States of America, 2000, Feb-01, Volume: 97, Issue:3

    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
Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.
    The Journal of general physiology, 2010, Volume: 136, Issue:3

    Topics: Animals; Cell Membrane Permeability; Chlorides; CHO Cells; Cricetinae; Cricetulus; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Ethyl Methanesulfonate; Ion Channel Gating; Kinetics; Membrane Potentials; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Patch-Clamp Techniques; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Transfection

2010
Manipulating the permeation of charged compounds through the MscL nanovalve.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011, Volume: 25, Issue:1

    Topics: Biological Transport; Cell Membrane; Chlorides; Electrophysiology; Escherichia coli; Escherichia coli Proteins; Glutamates; Ion Channel Gating; Ion Channels; Mesylates; Mutation; Nanopores; Potassium; Sodium; Spermine; Succinic Acid; Sulfhydryl Reagents; Trehalose

2011
The interaction of the gamma-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV.
    The Journal of biological chemistry, 2003, Oct-31, Volume: 278, Issue:44

    Topics: Amino Acid Sequence; Animals; Biological Transport; Biotinylation; Carrier Proteins; Chlorine; Cloning, Molecular; Dose-Response Relationship, Drug; Electrophysiology; GABA Plasma Membrane Transport Proteins; HeLa Cells; Humans; Kinetics; Membrane Proteins; Membrane Transport Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Organic Anion Transporters; Protein Binding; Protein Structure, Tertiary; RNA, Complementary; Sodium; Sulfhydryl Reagents; Transcription, Genetic; Transfection; Xenopus laevis

2003
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