ethyl methanesulfonate has been researched along with (2-sulfonatoethyl)methanethiosulfonate in 24 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 5 (20.83) | 18.2507 |
| 2000's | 18 (75.00) | 29.6817 |
| 2010's | 1 (4.17) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chen, JG; Rudnick, G; Sachpatzidis, A | 1 |
| Karlin, A; Zhang, H | 1 |
| Akabas, MH | 1 |
| Adams, CM; Price, MP; Snyder, PM; Welsh, MJ | 1 |
| Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Simpson, MM | 1 |
| Deng, HB; Guang, W; Wang, JB | 1 |
| Ball, SG; Balmforth, AJ; Fearon, IM; Palmer, AC; Peers, C; Varadi, G | 1 |
| Ennis, IL; Li, RA; Marbán, E; Tomaselli, GF; Vélez, P | 1 |
| Biber, J; Forster, IC; Lambert, G; Murer, H | 1 |
| Fozzard, HA; Glaaser, IW; Sunami, A | 1 |
| Beck, C; Kuner, T; Sakmann, B; Seeburg, PH | 1 |
| Ding, PZ; Wilson, TH | 1 |
| Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
| Cappello, AR; Daddabbo, L; Miniero, DV; Natuzzi, D; Palmieri, F; Stipani, I; Stipani, V | 1 |
| Giangregorio, N; Iacobazzi, V; Indiveri, C; Palmieri, F | 1 |
| Ashcroft, FM; Haider, S; Jones, P; Sansom, MS; Trapp, S | 1 |
| Huntley, SA; Krofchick, D; Silverman, M | 1 |
| Rudnick, G; Zhang, YW | 1 |
| Bhattacharyya, J; Enkvetchakul, D; Jeliazkova, I; Nichols, CG | 1 |
| Giangregorio, N; Indiveri, C; Palmieri, F; Tonazzi, A | 1 |
| Liu, T; Lo, B; Silverman, M; Speight, P | 1 |
| Abuladze, N; Azimov, R; Kao, L; Kurtz, I; Liu, W; Newman, D; Pushkin, A; Zhu, Q | 1 |
| Beaulieu, ME; Domazet, I; Escher, E; Guillemette, G; Holleran, BJ; Lavigne, P; Leduc, R; Yan, LP | 1 |
| Dempski, RE; Gaiko, O | 1 |
24 other study(ies) available for ethyl methanesulfonate and (2-sulfonatoethyl)methanethiosulfonate
| Article | Year |
|---|---|
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 |
Contribution of the beta subunit M2 segment to the ion-conducting pathway of the acetylcholine receptor.
Topics: Acetylcholine; Amino Acid Sequence; Amino Acid Substitution; Animals; Cysteine; Drug Synergism; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channels; Mesylates; Mice; Molecular Sequence Data; Mutagenesis, Insertional; Protein Structure, Secondary; Receptor, Muscarinic M2; Receptors, Muscarinic | 1998 |
Channel-lining residues in the M3 membrane-spanning segment of the cystic fibrosis transmembrane conductance regulator.
Topics: Animals; Chloride Channels; Cystic Fibrosis Transmembrane Conductance Regulator; Ethyl Methanesulfonate; Genetic Vectors; Humans; Ion Channel Gating; Membrane Proteins; Mesylates; Mutagenesis, Site-Directed; Oocytes; Peptide Fragments; Protein Structure, Secondary; Sequence Deletion; Water; Xenopus laevis | 1998 |
Protons activate brain Na+ channel 1 by inducing a conformational change that exposes a residue associated with neurodegeneration.
Topics: Amino Acid Substitution; Animals; Cold Temperature; Degenerin Sodium Channels; Epithelial Sodium Channels; Ethyl Methanesulfonate; Female; Indicators and Reagents; Ion Channel Gating; Ion Channels; Mesylates; Mutation; Nerve Tissue Proteins; Neurodegenerative Diseases; Neurons; Oocytes; Protein Conformation; Sodium Channels; Structure-Activity Relationship; Xenopus laevis | 1998 |
Electrostatic and aromatic microdomains within the binding-site crevice of the D2 receptor: contributions of the second membrane-spanning segment.
Topics: Amino Acid Substitution; Aspartic Acid; Binding, Competitive; Cell Line; Cell Membrane; Cysteine; Dopamine Antagonists; Ethyl Methanesulfonate; Humans; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments; Protein Binding; Protein Structure, Tertiary; Receptors, Dopamine D2; Static Electricity; Sulpiride | 1999 |
Selected cysteine residues in transmembrane domains of mu-opioid receptor are critical for effects of sulfhydryl reagents.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; CHO Cells; COS Cells; Cricetinae; Cysteine; Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; Ethyl Methanesulfonate; Humans; Ligands; Membranes; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Naloxone; Narcotic Antagonists; Radioligand Assay; Receptors, Opioid, mu; Sulfhydryl Reagents | 2000 |
Hypoxic and redox inhibition of the human cardiac L-type Ca2+ channel.
Topics: 4-Chloromercuribenzenesulfonate; Calcium Channel Blockers; Calcium Channels, L-Type; Cell Hypoxia; Cell Line; Dithiothreitol; Ethyl Methanesulfonate; Humans; Mesylates; Myocardium; Oxidation-Reduction; Recombinant Proteins; Transfection | 2000 |
Novel structural determinants of mu-conotoxin (GIIIB) block in rat skeletal muscle (mu1) Na+ channels.
Topics: Amino Acid Substitution; Animals; Aspartic Acid; Binding Sites; Cell Line; Conotoxins; Ethyl Methanesulfonate; Glutamic Acid; Humans; Kinetics; Mesylates; Models, Molecular; Muscle, Skeletal; Mutagenesis, Site-Directed; Protein Structure, Secondary; Rats; Sodium Channel Blockers; Sodium Channels; Transfection | 2000 |
Cysteine residues and the structure of the rat renal proximal tubular type II sodium phosphate cotransporter (rat NaPi IIa).
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cysteine; Disulfides; Ethyl Methanesulfonate; Kidney Tubules, Proximal; Mesylates; Methyl Methanesulfonate; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Tertiary; Rats; Reducing Agents; Serine; Sodium-Phosphate Cotransporter Proteins; Sodium-Phosphate Cotransporter Proteins, Type II; Sodium-Phosphate Cotransporter Proteins, Type IIa; Symporters; Xenopus laevis | 2000 |
Structural and gating changes of the sodium channel induced by mutation of a residue in the upper third of IVS6, creating an external access path for local anesthetics.
Topics: Amino Acid Substitution; Anesthetics, Local; Animals; Calcium Channel Blockers; Cells, Cultured; Conotoxins; Ethyl Methanesulfonate; Ion Channel Gating; Lidocaine; Mesylates; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Isoforms; Rats; Saxitoxin; Sodium Channel Blockers; Sodium Channels; Structure-Activity Relationship; Tetrodotoxin; Transfection; Xenopus laevis | 2001 |
Channel-lining residues of the AMPA receptor M2 segment: structural environment of the Q/R site and identification of the selectivity filter.
Topics: Amino Acid Substitution; Animals; Calcium; Cysteine; Cytoplasm; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Glutamic Acid; Ion Channel Gating; Kainic Acid; Kinetics; Membrane Potentials; Mesylates; Microinjections; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Permeability; Receptors, AMPA; Structure-Activity Relationship; Sulfhydryl Reagents; Xenopus laevis | 2001 |
The effect of modifications of the charged residues in the transmembrane helices on the transport activity of the melibiose carrier of Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Cell Membrane; Cysteine; Escherichia coli; Ethyl Methanesulfonate; Hydrogen Peroxide; Kinetics; Melibiose; Membrane Transport Proteins; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Recombinant Proteins; Sulfhydryl Reagents; Symporters | 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 |
The mitochondrial oxoglutarate carrier: cysteine-scanning mutagenesis of transmembrane domain IV and sensitivity of Cys mutants to sulfhydryl reagents.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Biological Transport, Active; Carrier Proteins; Cattle; Cysteine; Ethyl Methanesulfonate; Ethylmaleimide; Ketoglutaric Acids; Membrane Proteins; Membrane Transport Proteins; Mesylates; Mitochondria, Heart; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protein Structure, Tertiary; Proteolipids; Recombinant Proteins; Sulfhydryl Reagents | 2001 |
Site-directed mutagenesis and chemical modification of the six native cysteine residues of the rat mitochondrial carnitine carrier: implications for the role of cysteine-136.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cloning, Molecular; Cysteine; Escherichia coli; Ethyl Methanesulfonate; Ethylmaleimide; Mesylates; Mitochondria; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Organic Cation Transport Proteins; Protein Structure, Secondary; Rats; Recombinant Proteins; Solute Carrier Family 22 Member 5; Sulfhydryl Reagents | 2002 |
Identification of residues contributing to the ATP binding site of Kir6.2.
Topics: Adenosine Triphosphate; Animals; Arginine; Binding Sites; Ethyl Methanesulfonate; G Protein-Coupled Inwardly-Rectifying Potassium Channels; Lysine; Mesylates; Mice; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Potassium Channels, Inwardly Rectifying; Protein Structure, Secondary; Rats; Sulfhydryl Compounds; Sulfhydryl Reagents; Xenopus laevis | 2003 |
Position 170 of Rabbit Na+/glucose cotransporter (rSGLT1) lies in the Na+ pathway; modulation of polarity/charge at this site regulates charge transfer and carrier turnover.
Topics: Animals; Antigens, Viral, Tumor; Ethyl Methanesulfonate; Glutamine; Ion Channel Gating; Membrane Glycoproteins; Mesylates; Mice; Monosaccharide Transport Proteins; Mutation; Oocytes; Patch-Clamp Techniques; Phlorhizin; Rabbits; Sodium; Sodium-Glucose Transporter 1; Xenopus | 2004 |
Cysteine-scanning mutagenesis of serotonin transporter intracellular loop 2 suggests an alpha-helical conformation.
Topics: Amino Acid Sequence; Animals; Cysteine; Ethyl Methanesulfonate; HeLa Cells; Humans; Indicators and Reagents; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis; Nerve Tissue Proteins; Protein Structure, Secondary; Rats; Sequence Alignment; Serotonin; Serotonin Plasma Membrane Transport Proteins | 2005 |
Control of inward rectifier K channel activity by lipid tethering of cytoplasmic domains.
Topics: Bacterial Proteins; Burkholderia pseudomallei; Cell-Free System; Cloning, Molecular; Cysteine; Ethyl Methanesulfonate; Ion Channel Gating; Membrane Lipids; Mesylates; Methyl Methanesulfonate; Models, Molecular; Mutation; Potassium Channels, Inwardly Rectifying; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rubidium Radioisotopes; Sulfhydryl Reagents | 2007 |
Conformation-dependent accessibility of Cys-136 and Cys-155 of the mitochondrial rat carnitine/acylcarnitine carrier to membrane-impermeable SH reagents.
Topics: Animals; Biological Transport; Carnitine; Carnitine Acyltransferases; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Fluoresceins; Membrane Transport Proteins; Mesylates; Mitochondria; Models, Molecular; Mutant Proteins; Mutation; Permeability; Protein Conformation; Rats; Substrate Specificity; Sulfhydryl Reagents | 2007 |
Transmembrane IV of the high-affinity sodium-glucose cotransporter participates in sugar binding.
Topics: Alkylation; Animals; Carbohydrate Metabolism; Chlorocebus aethiops; COS Cells; Cricetinae; Cysteine; Ethyl Methanesulfonate; Female; Mesylates; Methylglucosides; Mutation, Missense; Oocytes; Patch-Clamp Techniques; Phlorhizin; Protein Structure, Tertiary; Rabbits; Sodium-Glucose Transporter 1; Xenopus laevis | 2008 |
NBCe1-A Transmembrane Segment 1 Lines the Ion Translocation Pathway.
Topics: Amino Acid Substitution; Bicarbonates; Cell Line; Ethyl Methanesulfonate; Humans; Ion Transport; Mesylates; Mutation, Missense; Protein Structure, Tertiary; Sodium; Sodium-Bicarbonate Symporters | 2009 |
Identification of transmembrane domain 6 & 7 residues that contribute to the binding pocket of the urotensin II receptor.
Topics: Alkylating Agents; Animals; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Ligands; Mesylates; Models, Molecular; Mutation; Polymerase Chain Reaction; Protein Binding; Protein Structure, Tertiary; Radioligand Assay; Rats; Receptors, G-Protein-Coupled; Transfection; Urotensins | 2009 |
Transmembrane domain three contributes to the ion conductance pathway of channelrhodopsin-2.
Topics: Amino Acid Sequence; Animals; Biological Transport; Cell Membrane; Ethyl Methanesulfonate; Extracellular Space; Female; Ions; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Permeability; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodopsin | 2013 |