Compounds > cocaine

cocaine and (2-(trimethylammonium)ethyl)methanethiosulfonate

cocaine has been researched along with (2-(trimethylammonium)ethyl)methanethiosulfonate in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (10.00)18.2507
2000's9 (90.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chen, JG; Rudnick, G; Sachpatzidis, A1
Chen, JG; Rudnick, G1
Androutsellis-Theotokis, A; Chen, JG; Huang, CJ; Moczydlowski, E; Ni, YG; Rudnick, G1
Androutsellis-Theotokis, A; Rudnick, G1
Gether, U; Loland, CJ; Norregaard, L1
Berfield, JL; Chen, N; Reith, ME; Rickey, J1
Johnsen, LB; Kristensen, AS; Larsen, MB; Wiborg, O1
Garcia, ML; Lee, E; Mitchell, SM; Stephan, MM1
Glomska, H; Keller, PC; Rudnick, G; Stephan, M1
Cao, J; Desai, RI; Gerstbrein, K; Gether, U; Grundt, P; Katz, JL; Loland, CJ; Newman, AH; Sitte, HH; Zou, MF1

Other Studies

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

ArticleYear
The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding.
    The Journal of biological chemistry, 1997, Nov-07, Volume: 272, Issue:45

    Topics: Asparagine; Binding Sites; Carrier Proteins; Cell Line; Cell Membrane; Cocaine; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Isoleucine; Ligands; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Structure, Secondary; Serotonin; Serotonin Plasma Membrane Transport Proteins; Structure-Activity Relationship; Tyrosine

1997
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
A lithium-induced conformational change in serotonin transporter alters cocaine binding, ion conductance, and reactivity of Cys-109.
    The Journal of biological chemistry, 2001, Aug-17, Volume: 276, Issue:33

    Topics: Animals; Carrier Proteins; Cocaine; Cysteine; Glutamates; HeLa Cells; Humans; Lithium; Membrane Glycoproteins; Membrane Potentials; Membrane Transport Proteins; Mesylates; Nerve Tissue Proteins; Protein Conformation; Serotonin Plasma Membrane Transport Proteins; Sodium; Xenopus

2001
Accessibility and conformational coupling in serotonin transporter predicted internal domains.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002, Oct-01, Volume: 22, Issue:19

    Topics: Amino Acid Sequence; Animals; Binding, Competitive; Carrier Proteins; Cell Membrane; Cocaine; Cysteine; Ethyl Methanesulfonate; HeLa Cells; Humans; Ions; Ligands; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Conformation; Protein Structure, Tertiary; Rats; Serotonin Plasma Membrane Transport Proteins; Structure-Activity Relationship; Sulfhydryl Reagents; Transfection

2002
Evidence for distinct sodium-, dopamine-, and cocaine-dependent conformational changes in transmembrane segments 7 and 8 of the dopamine transporter.
    The Journal of biological chemistry, 2003, Aug-15, Volume: 278, Issue:33

    Topics: Amino Acid Sequence; Animals; Cocaine; COS Cells; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Extracellular Space; Humans; Indicators and Reagents; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Conformation; Protein Structure, Tertiary; Radioligand Assay; Sodium; Tritium; Zinc

2003
Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation and cocaine binding.
    The Journal of biological chemistry, 2004, Feb-13, Volume: 279, Issue:7

    Topics: Alanine; Aspartic Acid; Biological Transport; Biotinylation; Blotting, Western; Cell Line; Cell Membrane; Cocaine; Cystine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Dose-Response Relationship, Drug; Glutamic Acid; Humans; Kinetics; Ligands; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Mutation; Nerve Tissue Proteins; Phenotype; Piperazines; Protein Binding; Protein Conformation; Protein Transport; Sodium; Time Factors; Zinc

2004
Mutational scanning of the human serotonin transporter reveals fast translocating serotonin transporter mutants.
    The European journal of neuroscience, 2004, Volume: 19, Issue:6

    Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Blotting, Western; Carrier Proteins; Chimera; Chlorocebus aethiops; Choline; Cloning, Molecular; Cocaine; COS Cells; Dose-Response Relationship, Drug; Humans; Indicators and Reagents; Inhibitory Concentration 50; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Radiopharmaceuticals; Serotonin; Serotonin Plasma Membrane Transport Proteins; Sodium; Structure-Activity Relationship; Transfection

2004
Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis.
    The Journal of biological chemistry, 2004, Jun-04, Volume: 279, Issue:23

    Topics: Animals; Binding Sites; Biological Transport; Biotinylation; Carrier Proteins; Cocaine; Cysteine; DNA, Complementary; Dose-Response Relationship, Drug; HeLa Cells; Humans; Indicators and Reagents; Ions; Kinetics; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protein Transport; Rats; Serotonin; Serotonin Plasma Membrane Transport Proteins; Structure-Activity Relationship; Zinc

2004
Cysteine-scanning mutagenesis of the fifth external loop of serotonin transporter.
    Biochemistry, 2004, Jul-06, Volume: 43, Issue:26

    Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Carrier Proteins; Cocaine; Cysteine; Dose-Response Relationship, Drug; Epitopes; HeLa Cells; Humans; Ions; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Sequence Homology, Amino Acid; Serotonin; Serotonin Plasma Membrane Transport Proteins; Sodium; Threonine

2004
Relationship between conformational changes in the dopamine transporter and cocaine-like subjective effects of uptake inhibitors.
    Molecular pharmacology, 2008, Volume: 73, Issue:3

    Topics: Alanine; Amino Acid Substitution; Animals; Biological Transport; Chlorocebus aethiops; Cocaine; COS Cells; Data Interpretation, Statistical; Discrimination Learning; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Dose-Response Relationship, Drug; Inhibitory Concentration 50; Male; Mesylates; Motor Activity; Protein Binding; Protein Conformation; Rats; Rats, Sprague-Dawley; Transfection

2008