(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with glycine in 11 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (glycine) | Trials (glycine) | Recent Studies (post-2010) (glycine) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 35,163 | 756 | 8,415 |
| Protein | Taxonomy | (2-(trimethylammonium)ethyl)methanethiosulfonate (IC50) | glycine (IC50) |
|---|---|---|---|
| Glutamate receptor ionotropic, NMDA 1 | Rattus norvegicus (Norway rat) | 1.4852 | |
| Sodium- and chloride-dependent glycine transporter 1 | Homo sapiens (human) | 106 | |
| Glutamate receptor ionotropic, NMDA 2A | Rattus norvegicus (Norway rat) | 0.3253 | |
| Glutamate receptor ionotropic, NMDA 2B | Rattus norvegicus (Norway rat) | 0.3253 | |
| Glutamate receptor ionotropic, NMDA 2C | Rattus norvegicus (Norway rat) | 0.3253 | |
| Glutamate receptor ionotropic, NMDA 2D | Rattus norvegicus (Norway rat) | 0.3253 | |
| Glutamate receptor ionotropic, NMDA 3B | Rattus norvegicus (Norway rat) | 0.3253 | |
| Glutamate receptor ionotropic, NMDA 3A | Rattus norvegicus (Norway rat) | 0.3253 | |
| Sodium- and chloride-dependent glycine transporter 2 | Homo sapiens (human) | 128 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 11 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Haddrill, JL; Lynch, JW; Shan, Q | 2 |
| Haddrill, J; Han, NL; Lynch, JW; Pierce, KD; Schofield, PR | 1 |
| Haddrill, JL; Han, NL; Lynch, JW | 1 |
| Absalom, NL; Kaplan, W; Lewis, TM; Pierce, KD; Schofield, PR | 1 |
| Dessen, A | 1 |
| Mazmanian, SK; Narayana, SV; Schneewind, O; Zong, Y | 1 |
| Clements, JD; Han, NL; Lynch, JW | 1 |
| Kanner, BI; Zhou, Y | 1 |
| Hawthorne, R; Lynch, JW | 1 |
| Chen, Z; Dillon, GH; Huang, R | 1 |
11 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and glycine
| Article | Year |
|---|---|
A single beta subunit M2 domain residue controls the picrotoxin sensitivity of alphabeta heteromeric glycine receptor chloride channels.
Topics: Allosteric Regulation; Amino Acid Substitution; Binding Sites; Binding, Competitive; Cell Line; Chloride Channels; Dose-Response Relationship, Drug; Glycine; Humans; Kidney; Mesylates; Mutagenesis, Site-Directed; Picrotoxin; Protein Structure, Tertiary; Protein Subunits; Receptors, Glycine; Sequence Homology, Amino Acid; Sulfhydryl Reagents | 2001 |
The surface accessibility of the glycine receptor M2-M3 loop is increased in the channel open state.
Topics: Amino Acid Substitution; Cell Line; Cysteine; Dithiothreitol; Dose-Response Relationship, Drug; Glycine; Humans; Ion Channel Gating; Kidney; Mesylates; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Protein Binding; Protein Conformation; Receptors, Glycine; Reducing Agents; Reflex, Startle; Transfection | 2001 |
Characterization of a glycine receptor domain that controls the binding and gating mechanisms of the beta-amino acid agonist, taurine.
Topics: Amino Acid Substitution; Binding Sites; Cell Line; Cysteine; Glycine; Humans; Ion Channel Gating; Kidney; Mesylates; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Receptors, Glycine; Sulfhydryl Reagents; Taurine | 2001 |
Comparative surface accessibility of a pore-lining threonine residue (T6') in the glycine and GABA(A) receptors.
Topics: Amino Acid Sequence; Animals; Cell Line; Copper; Cysteine; Disulfides; Dithiothreitol; Ethyl Methanesulfonate; GABA Antagonists; Glycine; Humans; Indicators and Reagents; Mesylates; Molecular Sequence Data; Mutation; Oocytes; Patch-Clamp Techniques; Phenanthrolines; Picrotoxin; Protein Subunits; Rats; Receptors, GABA-A; Receptors, Glycine; Sequence Alignment; Statistics as Topic; Sulfhydryl Reagents; Threonine; Xenopus laevis | 2002 |
Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.
Topics: Acetylcholine; Amino Acid Sequence; Carrier Proteins; Cysteine; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; Glycine; Humans; Indicators and Reagents; Ions; Ligands; Lysine; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Glycine; Sequence Homology, Amino Acid; Taurine; Time Factors | 2003 |
A new catalytic dyad regulates anchoring of molecules to the Gram-positive cell wall by sortases.
Topics: Amino Acid Motifs; Aminoacyltransferases; Anti-Infective Agents; Bacterial Proteins; Cell Wall; Cysteine; Cysteine Endopeptidases; Enzyme Inhibitors; Glycine; Mesylates; Peptidyl Transferases; Protein Structure, Tertiary; Protein Transport; Staphylococcus aureus | 2004 |
The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.
Topics: Amino Acid Motifs; Amino Acid Sequence; Aminoacyltransferases; Anti-Infective Agents; Bacterial Proteins; Cell Wall; Cysteine; Cysteine Endopeptidases; Enzyme Inhibitors; Glycine; Mesylates; Molecular Sequence Data; Peptidyl Transferases; Protein Structure, Tertiary; Protein Transport; Staphylococcus aureus | 2004 |
Comparison of taurine- and glycine-induced conformational changes in the M2-M3 domain of the glycine receptor.
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 |
Transporter-associated currents in the gamma-aminobutyric acid transporter GAT-1 are conditionally impaired by mutations of a conserved glycine residue.
Topics: Animals; Biotinylation; Conserved Sequence; Cysteine; Electric Conductivity; Female; GABA Plasma Membrane Transport Proteins; gamma-Aminobutyric Acid; Gene Expression; Glycine; HeLa Cells; Humans; Lithium; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Oocytes; Protein Conformation; RNA, Complementary; Sodium; Structure-Activity Relationship; Sulfhydryl Reagents; Transfection; Tritium; Xenopus laevis | 2005 |
A picrotoxin-specific conformational change in the glycine receptor M2-M3 loop.
Topics: Allosteric Site; Cyclopentanes; Cysteine; Dimerization; Diterpenes; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; Furans; Ginkgolides; Glycine; Humans; Inhibitory Concentration 50; Kinetics; Mesylates; Mutagenesis, Site-Directed; Mutation; Picrotoxin; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Glycine; Time Factors | 2005 |
Identification of residues critical for Cu2+-mediated inhibition of glycine alpha1 receptors.
Topics: Cell Line, Transformed; Cloning, Molecular; Copper; Dose-Response Relationship, Drug; Drug Interactions; Glycine; Histidine; Humans; Inhibitory Concentration 50; Membrane Potentials; Mesylates; Mutagenesis; Patch-Clamp Techniques; Receptors, Glycine; Sulfhydryl Reagents; Transfection; Zinc | 2006 |