Page last updated: 2024-09-02

(2-(trimethylammonium)ethyl)methanethiosulfonate and arginine

(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with arginine in 6 studies

Compound Research Comparison

Studies
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Trials
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Recent Studies (post-2010)
((2-(trimethylammonium)ethyl)methanethiosulfonate)
Studies
(arginine)
Trials
(arginine)
Recent Studies (post-2010) (arginine)
14301746,3881,68811,176

Protein Interaction Comparison

ProteinTaxonomy(2-(trimethylammonium)ethyl)methanethiosulfonate (IC50)arginine (IC50)
Cationic amino acid transporter 3Homo sapiens (human)283

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's5 (83.33)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR1
Dawson, DC; Liu, X; Smith, SS; Sun, F1
Alexeyev, MF; Winkler, HH1
Clements, JD; Han, NL; Lynch, JW1
Chikina, MD; Glaaser, IW; Hanck, DA; Lam, AD; McNulty, MM1
Cui, J; Delaloye, K; Nekouzadeh, A; Rudy, Y; Wu, D; Zaydman, MA1

Other Studies

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

ArticleYear
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
CFTR: covalent modification of cysteine-substituted channels expressed in Xenopus oocytes shows that activation is due to the opening of channels resident in the plasma membrane.
    The Journal of general physiology, 2001, Volume: 118, Issue:4

    Topics: Amino Acid Substitution; Animals; Arginine; Brefeldin A; Cell Membrane; Cyclic AMP; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Electric Conductivity; Female; Mesylates; Microinjections; Mutagenesis, Site-Directed; Oocytes; Protein Synthesis Inhibitors; RNA, Complementary; Time Factors; Xenopus

2001
Complete replacement of basic amino acid residues with cysteines in Rickettsia prowazekii ATP/ADP translocase.
    Biochimica et biophysica acta, 2002, Sep-20, Volume: 1565, Issue:1

    Topics: Amino Acids, Basic; Arginine; Cysteine; Cytoplasm; Kinetics; Lysine; Mesylates; Mitochondrial ADP, ATP Translocases; Mutagenesis, Site-Directed; Mutation; Periplasm; Protein Structure, Tertiary; Rickettsia prowazekii

2002
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
Role of Domain IV/S4 outermost arginines in gating of T-type calcium channels.
    Pflugers Archiv : European journal of physiology, 2005, Volume: 451, Issue:2

    Topics: Amino Acid Substitution; Arginine; Binding Sites; Calcium Channels, T-Type; Cell Line; Ethyl Methanesulfonate; Gene Expression; Humans; Hydrogen-Ion Concentration; Ion Channel Gating; Mesylates; Patch-Clamp Techniques; Sulfhydryl Reagents; Transfection

2005
State-dependent electrostatic interactions of S4 arginines with E1 in S2 during Kv7.1 activation.
    The Journal of general physiology, 2010, Volume: 135, Issue:6

    Topics: Amino Acid Sequence; Animals; Arginine; Cell Membrane; Cysteine; Ion Channel Gating; KCNQ1 Potassium Channel; Long QT Syndrome; Membrane Potentials; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Protein Structure, Tertiary; Protein Transport; Sulfhydryl Reagents; Surface Properties; Time Factors; Xenopus

2010