(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with cocaine in 10 studies
Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (cocaine) | Trials (cocaine) | Recent Studies (post-2010) (cocaine) |
---|---|---|---|---|---|
143 | 0 | 17 | 32,461 | 1,096 | 9,400 |
Protein | Taxonomy | (2-(trimethylammonium)ethyl)methanethiosulfonate (IC50) | cocaine (IC50) |
---|---|---|---|
Amyloid-beta precursor protein | Homo sapiens (human) | 0.338 | |
Fatty acid-binding protein, heart | Homo sapiens (human) | 0.367 | |
5-hydroxytryptamine receptor 2C | Rattus norvegicus (Norway rat) | 0.0855 | |
5-hydroxytryptamine receptor 2A | Rattus norvegicus (Norway rat) | 0.0855 | |
D | Rattus norvegicus (Norway rat) | 5.7544 | |
Alpha-2B adrenergic receptor | Rattus norvegicus (Norway rat) | 5.7544 | |
Alpha-2C adrenergic receptor | Rattus norvegicus (Norway rat) | 5.7544 | |
Alpha-2A adrenergic receptor | Rattus norvegicus (Norway rat) | 5.7544 | |
Sodium-dependent noradrenaline transporter | Homo sapiens (human) | 1.2861 | |
Sodium-dependent dopamine transporter | Rattus norvegicus (Norway rat) | 0.4321 | |
5-hydroxytryptamine receptor 2B | Rattus norvegicus (Norway rat) | 0.0855 | |
Sodium-dependent serotonin transporter | Homo sapiens (human) | 0.5442 | |
Sodium-dependent serotonin transporter | Rattus norvegicus (Norway rat) | 0.8885 | |
Sodium-dependent dopamine transporter | Homo sapiens (human) | 0.3796 | |
Potassium voltage-gated channel subfamily H member 2 | Homo sapiens (human) | 5.541 | |
Sodium-dependent dopamine transporter | Mus musculus (house mouse) | 0.2 | |
Sigma non-opioid intracellular receptor 1 | Homo sapiens (human) | 1.05 | |
Transporter | Rattus norvegicus (Norway rat) | 3.2277 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (10.00) | 18.2507 |
2000's | 9 (90.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
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Chen, JG; Rudnick, G; Sachpatzidis, A | 1 |
Chen, JG; Rudnick, G | 1 |
Androutsellis-Theotokis, A; Chen, JG; Huang, CJ; Moczydlowski, E; Ni, YG; Rudnick, G | 1 |
Androutsellis-Theotokis, A; Rudnick, G | 1 |
Gether, U; Loland, CJ; Norregaard, L | 1 |
Berfield, JL; Chen, N; Reith, ME; Rickey, J | 1 |
Johnsen, LB; Kristensen, AS; Larsen, MB; Wiborg, O | 1 |
Garcia, ML; Lee, E; Mitchell, SM; Stephan, MM | 1 |
Glomska, H; Keller, PC; Rudnick, G; Stephan, M | 1 |
Cao, J; Desai, RI; Gerstbrein, K; Gether, U; Grundt, P; Katz, JL; Loland, CJ; Newman, AH; Sitte, HH; Zou, MF | 1 |
10 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and cocaine
Article | Year |
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The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 |