(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with (2-sulfonatoethyl)methanethiosulfonate in 42 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies ((2-sulfonatoethyl)methanethiosulfonate) | Trials ((2-sulfonatoethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-sulfonatoethyl)methanethiosulfonate) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 86 | 0 | 12 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 6 (14.29) | 18.2507 |
| 2000's | 29 (69.05) | 29.6817 |
| 2010's | 7 (16.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chen, JG; Rudnick, G; Sachpatzidis, A | 1 |
| Fleischhauer, R; Lehmann-Horn, F; Lerche, H; Malina, T; Mitrovic, N; Peter, W; Pika-Hartlaub, U | 1 |
| Karlin, A; Zhang, H | 1 |
| Desai, RR; Fahlke, C; George, AL; Rhodes, TH | 1 |
| Freedman, ND; Grant, M; Hawrot, E; McLaughlin, JT; Russin, TS; Spura, A | 1 |
| Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Simpson, MM | 1 |
| del Camino, D; Holmgren, M; Liu, Y; Yellen, G | 1 |
| Deng, HB; Guang, W; Wang, JB | 1 |
| Fryklund, J; Hallén, S; Sachs, G | 1 |
| Biber, J; Forster, IC; Lambert, G; Murer, H | 1 |
| Haddrill, JL; Lynch, JW; Shan, Q | 1 |
| Fozzard, HA; Glaaser, IW; Sunami, A | 1 |
| Haddrill, J; Han, NL; Lynch, JW; Pierce, KD; Schofield, PR | 1 |
| Beck, C; Kuner, T; Sakmann, B; Seeburg, PH | 1 |
| Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
| Cance, P; Counillon, L; Lazdunski, M; Lingueglia, E; Poët, M; Poujeol, P; Tauc, M | 1 |
| Haddrill, JL; Han, NL; Lynch, JW | 1 |
| Cappello, AR; Daddabbo, L; Miniero, DV; Natuzzi, D; Palmieri, F; Stipani, I; Stipani, V | 1 |
| Banderali, U; Garneau, L; Hobeila, F; Klein, H; Parent, L; Roux, B; Sauvé, R; Simoes, M | 1 |
| Alexeyev, MF; Winkler, HH | 1 |
| Ding, PZ | 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 |
| Bartlett, MC; Clarke, DM; Loo, TW | 1 |
| Horrigan, FT; Zhang, G | 1 |
| Christie, DL; Dodd, JR | 1 |
| Alexander, C; Borg, E; Dawson, DC; Liu, X; Serrano, J | 1 |
| Bhattacharyya, J; Enkvetchakul, D; Jeliazkova, I; Nichols, CG | 1 |
| Khantwal, CM; Swaan, PW | 1 |
| Liu, T; Lo, B; Silverman, M; Speight, P | 1 |
| Ding, J; Fliegel, L; Li, X; Rainey, JK; Reddy, T; Sykes, BD | 1 |
| Abuladze, N; Azimov, R; Kao, L; Kurtz, I; Liu, W; Newman, D; Pushkin, A; Zhu, Q | 1 |
| Fliegel, L; Lee, BL; Li, X; Liu, Y; Sykes, BD | 1 |
| Fatehi, M; Linsdell, P | 1 |
| Herz, K; Kozachkov, L; Olkhova, E; Padan, E; Rimon, A | 1 |
| Cui, J; Delaloye, K; Nekouzadeh, A; Rudy, Y; Wu, D; Zaydman, MA | 1 |
| Mese, G; Sánchez, HA; Srinivas, M; Verselis, VK; White, TW | 1 |
| Fliegel, L; Lee, BL; Sykes, BD; Tzeng, J | 1 |
| Blount, P; Yang, LM | 1 |
| Kozachkov-Magrisso, L; Padan, E; Rimon, A | 1 |
| Furukawa, Y; Kodani, Y | 1 |
42 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate 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 |
Role in fast inactivation of the IV/S4-S5 loop of the human muscle Na+ channel probed by cysteine mutagenesis.
Topics: Adult; Amino Acid Substitution; Cell Line; Cysteine; Embryo, Mammalian; Humans; Indicators and Reagents; Kidney; Kinetics; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Protein Structure, Secondary; Sodium Channels; Sulfhydryl Reagents | 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 |
Pore stoichiometry of a voltage-gated chloride channel.
Topics: Cadmium; Cell Line; Chloride Channels; Cysteine; Electrochemistry; Histidine; Humans; Ion Channel Gating; Mesylates; Molecular Conformation; Muscle Proteins; Mutagenesis, Site-Directed; Phenanthrolines; Sulfhydryl Compounds | 1998 |
Probing the agonist domain of the nicotinic acetylcholine receptor by cysteine scanning mutagenesis reveals residues in proximity to the alpha-bungarotoxin binding site.
Topics: Acetylcholine; Animals; Bungarotoxins; Cysteine; Humans; Indicators and Reagents; Mesylates; Mice; Mutagenesis, Site-Directed; Nicotinic Agonists; Nicotinic Antagonists; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Protein Binding; Receptors, Nicotinic; Torpedo; Tryptophan; Valine | 1999 |
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 |
Blocker protection in the pore of a voltage-gated K+ channel and its structural implications.
Topics: Bacterial Proteins; Cysteine; Hydrogen Bonding; Intracellular Signaling Peptides and Proteins; Ion Channel Gating; Mesylates; Models, Molecular; Peptides; Potassium; Potassium Channel Blockers; Potassium Channels; Protein Conformation; Protein Structure, Secondary; Quaternary Ammonium Compounds; Shaker Superfamily of Potassium Channels; Static Electricity; Tetraethylammonium | 2000 |
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 |
Inhibition of the human sodium/bile acid cotransporters by side-specific methanethiosulfonate sulfhydryl reagents: substrate-controlled accessibility of site of inactivation.
Topics: Amino Acid Sequence; Animals; Bile Acids and Salts; Biological Transport; Carrier Proteins; Cell Line; Enzyme Inhibitors; Humans; Kinetics; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Organic Anion Transporters, Sodium-Dependent; Sulfhydryl Reagents; Symporters; Taurocholic Acid; 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 |
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 |
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 |
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 |
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 |
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 |
Exploration of the pore structure of a peptide-gated Na+ channel.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cell Line; Cysteine; DNA, Complementary; Female; FMRFamide; Humans; Ion Channel Gating; Ion Transport; Mesylates; Models, Molecular; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Oocytes; Protein Conformation; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Sodium; Sodium Channels; Static Electricity; Sulfhydryl Reagents; Xenopus laevis | 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 |
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 |
Cysteine mutagenesis and computer modeling of the S6 region of an intermediate conductance IKCa channel.
Topics: Animals; Computers; Cysteine; Electric Conductivity; Female; HeLa Cells; Humans; Mesylates; Models, Biological; Models, Genetic; Mutagenesis; Oocytes; Potassium Channels, Calcium-Activated; Sequence Homology; Sulfhydryl Reagents; Xenopus laevis | 2002 |
Complete replacement of basic amino acid residues with cysteines in Rickettsia prowazekii ATP/ADP translocase.
Topics: Amino Acids, Basic; Arginine; Cysteine; Cytoplasm; Kinetics; Lysine; Mesylates; Mitochondrial ADP, ATP Translocases; Mutagenesis, Site-Directed; Mutation; Periplasm; Protein Structure, Tertiary; Rickettsia prowazekii | 2002 |
An investigation of cysteine mutants on the cytoplasmic loop X/XI in the melibiose transporter of Escherichia coli by using thiol reagents: implication of structural conservation of charged residues.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acids; Animals; Biological Transport; Cells, Cultured; Cysteine; Escherichia coli Proteins; Iodoacetic Acid; Melibiose; Mesylates; Mutation; Protein Structure, Secondary; Sulfhydryl Reagents; Symporters | 2003 |
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 |
The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding Sites; Biological Transport; Buffers; Cell Line; Colchicine; Cyclosporine; Cysteine; Drug Resistance, Multiple; Gene Expression Regulation; Humans; Hydrolysis; Isoleucine; Mesylates; Mutation; Rhodamines; Verapamil; Water | 2004 |
Cysteine modification alters voltage- and Ca(2+)-dependent gating of large conductance (BK) potassium channels.
Topics: Animals; Calcium; Cysteine; Electrophysiology; Humans; Indicators and Reagents; Ion Channel Gating; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits; Large-Conductance Calcium-Activated Potassium Channels; Mesylates; Mice; Potassium Channels, Calcium-Activated | 2005 |
Substituted cysteine accessibility of the third transmembrane domain of the creatine transporter: defining a transport pathway.
Topics: Amino Acid Sequence; Binding Sites; Biological Transport; Biotinylation; Cell Line; Cell Membrane; Chlorine; Creatine; Cysteine; Dose-Response Relationship, Drug; Humans; Ions; Membrane Transport Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis; Mutation; Protein Binding; Protein Structure, Tertiary; Sodium; Solvents; Sulfhydryl Reagents; Time Factors; Transfection | 2005 |
Variable reactivity of an engineered cysteine at position 338 in cystic fibrosis transmembrane conductance regulator reflects different chemical states of the thiol.
Topics: Alkylating Agents; Animals; Catalysis; Copper; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Disulfides; Dithiothreitol; Glutathione; Humans; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iodoacetamide; Mercaptoethanol; Mesylates; Metals; Models, Biological; Oocytes; Oxygen; Phenotype; Protein Engineering; Sulfhydryl Compounds; Sulfinic Acids; Sulfonic Acids; Time Factors; Xenopus | 2006 |
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 |
Cytosolic half of transmembrane domain IV of the human bile acid transporter hASBT (SLC10A2) forms part of the substrate translocation pathway.
Topics: Amino Acid Sequence; Animals; Chlorocebus aethiops; Computational Biology; COS Cells; Cysteine; Cytosol; Humans; Mesylates; Models, Molecular; Molecular Sequence Data; Organic Anion Transporters, Sodium-Dependent; Point Mutation; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Symporters | 2008 |
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 |
Structural and functional characterization of transmembrane segment IX of the NHE1 isoform of the Na+/H+ exchanger.
Topics: Cation Transport Proteins; Cations; Cell Line, Tumor; Circular Dichroism; Cysteine; Gene Expression Regulation; Humans; Magnetic Resonance Spectroscopy; Mesylates; Micelles; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptides; Protein Isoforms; Protein Structure, Tertiary; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers; Sulfhydryl Reagents | 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 |
Structural and functional analysis of transmembrane XI of the NHE1 isoform of the Na+/H+ exchanger.
Topics: Cation Transport Proteins; Escherichia coli; Humans; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Mesylates; Micelles; Molecular Conformation; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Peptides; Protein Conformation; Protein Structure, Tertiary; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers | 2009 |
Novel residues lining the CFTR chloride channel pore identified by functional modification of introduced cysteines.
Topics: Amino Acid Sequence; Animals; Cricetinae; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Humans; Mesylates; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Sulfhydryl Reagents | 2009 |
Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.
Topics: Aspartic Acid; Cations; Cell Membrane; Computer Simulation; Conserved Sequence; Crystallography, X-Ray; Cysteine; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Hydrogen-Ion Concentration; Ion Transport; Lithium; Mesylates; Models, Molecular; Mutation; Periplasm; Phenotype; Protein Conformation; Sodium-Hydrogen Exchangers | 2010 |
State-dependent electrostatic interactions of S4 arginines with E1 in S2 during Kv7.1 activation.
Topics: Amino Acid Sequence; Animals; Arginine; Cell Membrane; Cysteine; Ion Channel Gating; KCNQ1 Potassium Channel; Long QT Syndrome; Membrane Potentials; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Protein Structure, Tertiary; Protein Transport; Sulfhydryl Reagents; Surface Properties; Time Factors; Xenopus | 2010 |
Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome.
Topics: Amino Acid Substitution; Animals; Barium; Calcium; Cell Line, Tumor; Chelating Agents; Chloride Channels; Connexin 26; Connexins; Cysteine; Deafness; Electrophysiological Phenomena; Ethylenediamines; Gap Junctions; Humans; Ion Channel Gating; Keratitis; Membrane Potentials; Mesylates; Mice; Mutation, Missense; Oocytes; Permeability; RNA, Messenger; Streptomyces; Sulfhydryl Reagents; Syndrome; Transfection; Xenopus laevis | 2010 |
Structural and functional analysis of transmembrane segment VI of the NHE1 isoform of the Na+/H+ exchanger.
Topics: Cation Transport Proteins; Cell Membrane; Cysteine; Humans; Immunoblotting; Magnetic Resonance Spectroscopy; Mesylates; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Isoforms; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers; Structure-Activity Relationship | 2010 |
Manipulating the permeation of charged compounds through the MscL nanovalve.
Topics: Biological Transport; Cell Membrane; Chlorides; Electrophysiology; Escherichia coli; Escherichia coli Proteins; Glutamates; Ion Channel Gating; Ion Channels; Mesylates; Mutation; Nanopores; Potassium; Sodium; Spermine; Succinic Acid; Sulfhydryl Reagents; Trehalose | 2011 |
The unwound portion dividing helix IV of NhaA undergoes a conformational change at physiological pH and lines the cation passage.
Topics: Amino Acid Substitution; Cations; Cell Membrane Permeability; Escherichia coli; Escherichia coli Proteins; Mesylates; Models, Molecular; Protein Structure, Secondary; Sodium-Hydrogen Exchangers | 2012 |
Electrostatic charge at position 552 affects the activation and permeation of FMRFamide-gated Na+ channels.
Topics: Animals; Aplysia; Cysteine; Dose-Response Relationship, Drug; FMRFamide; Ion Channel Gating; Membrane Potentials; Mesylates; Models, Molecular; Mutation; Nerve Tissue Proteins; Oocytes; Permeability; Protein Conformation; Sodium; Sodium Channels; Static Electricity; Surface Properties; Xenopus laevis | 2014 |