ethyl methanesulfonate has been researched along with methanethiosulfonate in 13 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (15.38) | 18.2507 |
| 2000's | 9 (69.23) | 29.6817 |
| 2010's | 2 (15.38) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chen, J; Fu, D; Javitch, JA; Karlin, A | 1 |
| Chen, J; Fu, D; Javitch, JA | 1 |
| Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Xu, W | 1 |
| Liu, J; Siegelbaum, SA | 1 |
| Loussouarn, G; Masia, R; Nichols, CG; Phillips, LR; Rose, T | 1 |
| Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
| Christie, DL; Dodd, JR | 1 |
| Torres, VI; Weiss, DS | 1 |
| Beaulieu, ME; Boucard, AA; Escher, E; Guillemette, G; Lavigne, P; Leduc, R; Roy, M | 1 |
| Alexeyev, MF; Audia, JP; Daugherty, RM; Roberts, RA; Winkler, HH | 1 |
| Banerjee, A; Hussainzada, N; Swaan, PW | 1 |
| Chen, TY; Yu, WP; Zhang, XD | 1 |
| Barajas-MartÃnez, H; Biet, M; Delabre, JF; Dumaine, R; Morin, N; Ton, AT | 1 |
13 other study(ies) available for ethyl methanesulfonate and methanethiosulfonate
| Article | Year |
|---|---|
Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method.
Topics: Binding Sites; Cell Line; Cysteine; Embryo, Mammalian; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Kidney; Mesylates; Mutagenesis, Site-Directed; Peptide Mapping; Protein Structure, Secondary; Quaternary Ammonium Compounds; Receptors, Dopamine D2; Transfection | 1995 |
Residues in the fifth membrane-spanning segment of the dopamine D2 receptor exposed in the binding-site crevice.
Topics: Amino Acid Sequence; Binding Sites; Cysteine; Dopamine Antagonists; Dopamine D2 Receptor Antagonists; Drug Resistance; Ethyl Methanesulfonate; Humans; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Receptors, Dopamine D2; Spiperone; Sulpiride; Transfection | 1995 |
The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the mu, delta, and kappa opioid receptors.
Topics: Amino Acid Sequence; Animals; Benzomorphans; Binding Sites; Cell Line; Conserved Sequence; Cysteine; Diprenorphine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Glutamic Acid; Humans; Indicators and Reagents; Mesylates; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Naloxone; Narcotic Antagonists; Protein Structure, Secondary; Rats; Receptors, Opioid; Receptors, Opioid, delta; Receptors, Opioid, kappa; Receptors, Opioid, mu; Serine; Time Factors; Tritium | 2000 |
Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels.
Topics: Animals; Bacterial Proteins; Cattle; Cells, Cultured; Cyclic Nucleotide-Gated Cation Channels; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channel Gating; Ion Channels; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Potassium Channels; Protein Conformation; Protein Structure, Secondary; Retinal Rod Photoreceptor Cells; Sequence Homology, Amino Acid; Sulfhydryl Reagents; Water; Xenopus | 2000 |
Flexibility of the Kir6.2 inward rectifier K(+) channel pore.
Topics: Amino Acid Sequence; Animals; Cadmium; COS Cells; Cysteine; Dimerization; Ethyl Methanesulfonate; Indicators and Reagents; Mesylates; Methyl Methanesulfonate; Models, Biological; Models, Molecular; Molecular Sequence Data; Pliability; Point Mutation; Potassium Channel Blockers; Potassium Channels; Potassium Channels, Inwardly Rectifying; Protein Conformation; Quaternary Ammonium Compounds; Sequence Homology, Amino Acid | 2001 |
CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.
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 |
Cysteine 144 in the third transmembrane domain of the creatine transporter is located close to a substrate-binding site.
Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Biotinylation; Cattle; Cell Line; Chlorine; Creatine; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ions; Kinetics; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rabbits; Rats; Sequence Homology, Amino Acid; Serine; Sodium; Transfection | 2001 |
Identification of a tyrosine in the agonist binding site of the homomeric rho1 gamma-aminobutyric acid (GABA) receptor that, when mutated, produces spontaneous opening.
Topics: Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Crotonates; Dimerization; Dose-Response Relationship, Drug; Electrophysiology; Ethyl Methanesulfonate; GABA Antagonists; Glycine; Humans; Imidazoles; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Organophosphorus Compounds; Picrotoxin; Protein Binding; Receptors, GABA-B; RNA, Complementary; Serine; Transcription, Genetic; Tryptophan; Tyrosine; Xenopus laevis | 2002 |
Constitutive activation of the angiotensin II type 1 receptor alters the spatial proximity of transmembrane 7 to the ligand-binding pocket.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cell Membrane; COS Cells; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Genes, Reporter; Humans; Isoleucine; Kinetics; Ligands; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Receptor, Angiotensin, Type 1; Sequence Homology, Amino Acid; Transfection; Tyrosine; Water | 2003 |
Cysteine-scanning mutagenesis and thiol modification of the Rickettsia prowazekii ATP/ADP translocase: evidence that transmembrane regions I and II, but not III, are structural components of the aqueous translocation channel.
Topics: Amino Acid Sequence; Amino Acid Substitution; Cysteine; Ethyl Methanesulfonate; Ion Channel Gating; Isoleucine; Mesylates; Mitochondrial ADP, ATP Translocases; Molecular Sequence Data; Mutagenesis; Mutation; Phenylalanine; Rickettsia prowazekii; Sequence Homology, Amino Acid; Sulfhydryl Compounds; Translocation, Genetic; Tyrosine | 2004 |
Transmembrane domain VII of the human apical sodium-dependent bile acid transporter ASBT (SLC10A2) lines the substrate translocation pathway.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Biological Transport; Cell Membrane; Chlorocebus aethiops; Computational Biology; COS Cells; Cysteine; Ethyl Methanesulfonate; Humans; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutant Proteins; Organic Anion Transporters, Sodium-Dependent; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Sodium; Solvents; Structure-Activity Relationship; Substrate Specificity; Symporters | 2006 |
Accessibility of the CLC-0 pore to charged methanethiosulfonate reagents.
Topics: Amino Acid Sequence; Animals; Cell Line; Chloride Channels; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Kinetics; Mesylates; Models, Chemical; Patch-Clamp Techniques; Point Mutation; Protein Structure, Quaternary; Torpedo | 2010 |
About half of the late sodium current in cardiac myocytes from dog ventricle is due to non-cardiac-type Na(+) channels.
Topics: Action Potentials; Animals; Cell Line; Dogs; Ethyl Methanesulfonate; Heart Ventricles; Membrane Potentials; Mesylates; Myocytes, Cardiac; NAV1.5 Voltage-Gated Sodium Channel; Patch-Clamp Techniques; Tetrodotoxin; Voltage-Gated Sodium Channel Blockers | 2012 |