(2-(trimethylammonium)ethyl)methanethiosulfonate has been researched along with cysteine in 94 studies
| Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate) | Studies (cysteine) | Trials (cysteine) | Recent Studies (post-2010) (cysteine) |
|---|---|---|---|---|---|
| 143 | 0 | 17 | 40,132 | 418 | 11,457 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 10 (10.64) | 18.2507 |
| 2000's | 72 (76.60) | 29.6817 |
| 2010's | 12 (12.77) | 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 |
| Cao, Y; Lester, HA; Mager, S; Yu, N | 1 |
| Karlin, A; Zhang, H | 1 |
| Desai, RR; Fahlke, C; George, AL; Rhodes, TH | 1 |
| Armstrong, CM; Khodakhah, K; Melishchuk, A | 1 |
| Kriegler, S; Sudweeks, S; Yakel, JL | 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 |
| Becchetti, A; Gamel, K; Torre, V | 1 |
| Bai, G; Chen, HS; Choi, YB; Le, DA; Lipton, SA; Ortiz, J; Tenneti, L | 1 |
| del Camino, D; Holmgren, M; Liu, Y; Yellen, G | 1 |
| Pang, T; Shigekawa, M; Su, X; Wakabayashi, S | 1 |
| Deng, HB; Guang, W; Wang, JB | 1 |
| Brauer, D; Dean, AM; Kaplan, RS; Kotaria, R; Mayor, JA; Walters, DE | 1 |
| Cohen, JB; Sullivan, DA | 1 |
| Hill, BJ; Huang, L; Milanick, MA; Parkinson, EL; Wilson, BJ; Xu, W | 1 |
| George, AL; Horn, R; Mitrovic, N | 1 |
| Biber, J; Forster, IC; Lambert, G; Murer, H | 1 |
| Lamb, RA; Pinto, LH; Shuck, K | 1 |
| Haddrill, J; Han, NL; Lynch, JW; Pierce, KD; Schofield, PR | 1 |
| Pajor, AM | 1 |
| Beck, C; Kuner, T; Sakmann, B; Seeburg, PH | 1 |
| Androutsellis-Theotokis, A; Chen, JG; Huang, CJ; Moczydlowski, E; Ni, YG; Rudnick, G | 1 |
| Lynch, JW; Seebungkert, B | 1 |
| Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
| Dawson, DC; Liu, X; Smith, SS; Sun, F | 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 |
| Cui, Y; Fan, Z; Wang, W | 1 |
| Chiara, DC; Cohen, JB; Sullivan, D | 1 |
| Collier, RJ; Finkelstein, A; Nassi, S | 1 |
| Arrabit, C; Cruz, H; Panicker, S; Slesinger, PA | 1 |
| Clyne, JD; Hume, RI; Wang, LF | 1 |
| Banderali, U; Garneau, L; Hobeila, F; Klein, H; Parent, L; Roux, B; Sauvé, R; Simoes, M | 1 |
| Alexeyev, MF; Winkler, HH | 1 |
| Haddrill, JL; Lynch, JW; Shan, Q | 1 |
| Androutsellis-Theotokis, A; Rudnick, G | 1 |
| Björquist, A; Hallén, S; Ostlund-Lindqvist, AM; Sachs, G | 1 |
| Dehaye, JP; Nagy, A; Premkumar, A; Turner, RJ | 1 |
| Goldstein, SA; Gonzalez-Colaso, R; Nikolaeva, N; Rajan, S; Sesti, F | 1 |
| Busch, A; Fann, MC; Maloney, PC | 1 |
| Xiao, J; Yang, J; Zhen, XG | 1 |
| Ding, PZ | 1 |
| Cahill, H; Nathans, J; Smallwood, P; Sun, H; Tsunenari, T; Williams, J; Yau, KW | 1 |
| Ding, XQ; Dolu, V; Hadac, EM; Miller, LJ; Schuetz, M | 1 |
| Absalom, NL; Kaplan, W; Lewis, TM; Pierce, KD; Schofield, PR | 1 |
| Boggs, JM; Culham, DE; Henderson, J; Hillar, A; Ly, A; Racher, KI; Vernikovska, YI; Wood, JM | 1 |
| Haworth, IS; Kulkarni, AA; Lee, VH; Uchiyama, T | 1 |
| Clark, E; Gandhi, CS; Isacoff, EY; Loots, E; Pralle, A | 1 |
| Bell, DC; Riley, JH; Saenger, RC; Siegelbaum, SA; Yao, H | 1 |
| Dessen, A | 1 |
| Mazmanian, SK; Narayana, SV; Schneewind, O; Zong, Y | 1 |
| Casey, JR; Zhu, Q | 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 |
| Amster-Choder, O; Yagur-Kroll, S | 1 |
| Pajor, AM; Randolph, KM | 1 |
| Kanner, BI; Zhou, Y | 1 |
| Dellal, SS; Hume, RI; Nagaya, N; Saar, N; Tittle, RK | 1 |
| Christie, DL; Dodd, JR | 1 |
| Bryan-Lluka, LJ; Sucic, S | 1 |
| Hawthorne, R; Lynch, JW | 1 |
| Fitzmaurice, A; Orenstein, ET; Schoonover, CE; Xie, C; Yang, J; Zhen, XG | 1 |
| Xie, C; Yang, J; Zhen, XG | 1 |
| Kanner, BI; Shachnai, L; Shimamoto, K | 1 |
| Alexander, C; Borg, E; Dawson, DC; Liu, X; Serrano, J | 1 |
| Covarrubias, M; Wang, G | 1 |
| Kanner, BI; Shlaifer, I | 1 |
| Banderali, U; Garneau, L; Klein, H; Parent, L; Sauvé, R; Simoes, M | 1 |
| Davies, DL; Haworth, IS; Kulkarni, AA; Lee, VH; Links, JL | 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 |
| Chang, TH; Li, M; Silberberg, SD; Swartz, KJ | 1 |
| Joshi, AD; Pajor, AM | 1 |
| Fatehi, M; Linsdell, P | 1 |
| Herz, K; Kozachkov, L; Olkhova, E; Padan, E; Rimon, A | 1 |
| Engh, A; McNally, BA; Prakriya, M; Yamashita, M | 1 |
| Kurata, HT; Nichols, CG; Zhu, EA | 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 |
| El Hiani, Y; Linsdell, P | 1 |
| Bai, Y; Hwang, TC; Li, M | 1 |
| Fliegel, L; Lee, BL; Sykes, BD; Tzeng, J | 1 |
| Roberts, DJ; Vertongen, P; Waelbroeck, M | 1 |
| Anderson, CM; Choi, YE; Eskandari, S; Maestas, MJ; Omoto, JJ; Rahnama-Vaghef, A; Salto, G; Sanchez, RV | 1 |
| Jiang, Y; John, SA; Liao, J; Ottolia, M | 1 |
| Furukawa, Y; Kodani, Y | 1 |
| Li, J; Pei, L; Rajagopal, M; Yu, ASL; Zhuo, M | 1 |
94 other study(ies) available for (2-(trimethylammonium)ethyl)methanethiosulfonate and cysteine
| 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 |
Topological localization of cysteine 74 in the GABA transporter, GAT1, and its importance in ion binding and permeation.
Topics: Animals; Biological Transport; Carrier Proteins; Cysteine; Electrophysiology; Extracellular Space; GABA Plasma Membrane Transport Proteins; gamma-Aminobutyric Acid; Membrane Glycoproteins; Membrane Proteins; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Organic Anion Transporters; Patch-Clamp Techniques; Structure-Activity Relationship; Sulfhydryl Reagents; Xenopus laevis | 1998 |
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 |
Charge immobilization caused by modification of internal cysteines in squid Na channels.
Topics: Anesthetics, Local; Animals; Axons; Biophysical Phenomena; Biophysics; Cysteine; Decapodiformes; In Vitro Techniques; Ion Channel Gating; Kinetics; Membrane Potentials; Mesylates; Perfusion; Sodium Channels | 1998 |
The nicotinic alpha4 receptor subunit contributes to the lining of the ion channel pore when expressed with the 5-HT3 receptor subunit.
Topics: Animals; Cysteine; Genetic Engineering; Indicators and Reagents; Mesylates; Oocytes; Receptors, Nicotinic; Receptors, Serotonin; Receptors, Serotonin, 5-HT3; Silver Nitrate; Xenopus | 1999 |
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 |
Cyclic nucleotide-gated channels. Pore topology studied through the accessibility of reporter cysteines.
Topics: Amino Acid Sequence; Animals; Cell Membrane; Cysteine; Ethyl Methanesulfonate; Genes, Reporter; Ion Channel Gating; Ion Channels; Membrane Potentials; Mesylates; Molecular Sequence Data; Mutagenesis; Nucleotides, Cyclic; Oocytes; Patch-Clamp Techniques; Xenopus laevis | 1999 |
Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation.
Topics: Animals; Cell Line; Chromatography, High Pressure Liquid; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ion Transport; Mesylates; Mutagenesis, Site-Directed; N-Methylaspartate; Nitric Oxide; Nitroso Compounds; Oocytes; Patch-Clamp Techniques; Peptide Fragments; Receptors, N-Methyl-D-Aspartate; S-Nitrosothiols; Transfection; Xenopus laevis | 2000 |
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 |
A novel topology model of the human Na(+)/H(+) exchanger isoform 1.
Topics: Amino Acid Sequence; Biological Transport; Biotinylation; Cell Membrane Permeability; Cysteine; Humans; Maleimides; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Isoforms; Protein Structure, Tertiary; Sodium-Hydrogen Exchangers; Sulfhydryl Reagents; Surface Properties | 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 |
The yeast mitochondrial citrate transport protein. Probing the secondary structure of transmembrane domain iv and identification of residues that likely comprise a portion of the citrate translocation pathway.
Topics: Amino Acid Sequence; Amino Acid Substitution; Carrier Proteins; Cysteine; Escherichia coli; Ethyl Methanesulfonate; Fungal Proteins; Indicators and Reagents; Mesylates; Mitochondria; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary | 2000 |
Mapping the agonist binding site of the nicotinic acetylcholine receptor. Orientation requirements for activation by covalent agonist.
Topics: Acetylcholine; Affinity Labels; Alkylation; Animals; Binding Sites; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Indicators and Reagents; Kinetics; Mesylates; Models, Chemical; Mutagenesis; Nicotinic Agonists; Patch-Clamp Techniques; Protein Structure, Quaternary; Quaternary Ammonium Compounds; Receptors, Nicotinic; Time Factors; Transcription, Genetic; Xenopus | 2000 |
Probing the extracellular release site of the plasma membrane calcium pump.
Topics: Binding Sites; Cadmium; Calcium Signaling; Calcium-Transporting ATPases; Cysteine; Erythrocyte Membrane; Ethyl Methanesulfonate; Extracellular Space; Histidine; Humans; In Vitro Techniques; Ion Transport; Membrane Potentials; Mesylates; Models, Biological; Protons | 2000 |
Role of domain 4 in sodium channel slow inactivation.
Topics: Cell Line, Transformed; Cysteine; Electric Stimulation; Humans; Indicators and Reagents; Ion Channel Gating; Kidney; Membrane Potentials; Mesylates; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Protein Structure, Tertiary; Sodium Channels | 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 |
Analysis of the pore structure of the influenza A virus M(2) ion channel by the substituted-cysteine accessibility method.
Topics: Amino Acid Substitution; Animals; Cysteine; In Vitro Techniques; Indicators and Reagents; Influenza A virus; Ion Channels; Membrane Proteins; Mesylates; Models, Molecular; Mutation; Oocytes; Patch-Clamp Techniques; Protein Structure, Tertiary; Sequence Analysis, Protein; Viral Matrix Proteins; Xenopus laevis | 2000 |
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 |
Conformationally sensitive residues in transmembrane domain 9 of the Na+/dicarboxylate co-transporter.
Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Blotting, Western; Carrier Proteins; Cations; Cell Membrane; Cysteine; Dicarboxylic Acid Transporters; Dose-Response Relationship, Drug; Electrophysiology; Indicators and Reagents; Kinetics; Membrane Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Oocytes; Organic Anion Transporters, Sodium-Dependent; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Symporters; Time Factors; Xenopus | 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 |
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 |
A common inhibitory binding site for zinc and odorants at the voltage-gated K(+) channel of rat olfactory receptor neurons.
Topics: 4-Chloromercuribenzenesulfonate; Acetophenones; Animals; Binding Sites; Carbon Monoxide; Cells, Cultured; Cyclohexenes; Cysteine; Diethyl Pyrocarbonate; Dose-Response Relationship, Drug; Histidine; Limonene; Membrane Potentials; Mesylates; Neural Inhibition; Nitric Oxide; Olfactory Receptor Neurons; Patch-Clamp Techniques; Pentanols; Potassium; Potassium Channels; Rats; Receptors, Odorant; Smell; Sulfhydryl Reagents; Terpenes; Zinc | 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 |
CFTR: covalent modification of cysteine-substituted channels expressed in Xenopus oocytes shows that activation is due to the opening of channels resident in the plasma membrane.
Topics: Amino Acid Substitution; Animals; Arginine; Brefeldin A; Cell Membrane; Cyclic AMP; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Electric Conductivity; Female; Mesylates; Microinjections; Mutagenesis, Site-Directed; Oocytes; Protein Synthesis Inhibitors; RNA, Complementary; Time Factors; 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 |
Cytoplasmic vestibule of the weak inward rectifier Kir6.2 potassium channel.
Topics: Adenosine Triphosphate; Animals; Cells, Cultured; COS Cells; Cysteine; Cytoplasm; DNA, Complementary; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Immunohistochemistry; Isoleucine; Mesylates; Models, Biological; Models, Chemical; Mutagenesis, Site-Directed; Naphthalenesulfonates; Patch-Clamp Techniques; Potassium; Potassium Channels, Inwardly Rectifying; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Recombinant Fusion Proteins; Serine; Spermine; Sulfhydryl Reagents; Transfection | 2002 |
Mapping the agonist binding site of the nicotinic acetylcholine receptor by cysteine scanning mutagenesis: antagonist footprint and secondary structure prediction.
Topics: Amino Acid Substitution; Animals; Binding, Competitive; Cysteine; Ethyl Methanesulfonate; Mesylates; Mutagenesis; Nicotinic Agonists; Oocytes; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Nicotinic; Torpedo; Xenopus laevis | 2002 |
PA63 channel of anthrax toxin: an extended beta-barrel.
Topics: Antigens, Bacterial; Bacillus anthracis; Bacterial Toxins; Cysteine; Ion Channel Gating; Ion Channels; Lipid Bilayers; Mesylates; Mutagenesis, Site-Directed; Protein Structure, Secondary; Quaternary Ammonium Compounds | 2002 |
Evidence for a centrally located gate in the pore of a serotonin-gated ion channel.
Topics: Amino Acid Substitution; Animals; Cysteine; DNA, Complementary; Ethyl Methanesulfonate; Ion Channel Gating; Ligands; Mesylates; Mice; Microinjections; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Conformation; Protein Structure, Tertiary; Receptors, Serotonin; Receptors, Serotonin, 5-HT3; Sequence Analysis, DNA; Serotonin; Structure-Activity Relationship; Xenopus | 2002 |
Mutational analysis of the conserved cysteines of the rat P2X2 purinoceptor.
Topics: Adenosine Triphosphate; Animals; Cell Line; Conserved Sequence; Cysteine; Dithiothreitol; DNA Mutational Analysis; Dose-Response Relationship, Drug; Humans; Kidney; Membrane Potentials; Mesylates; Mutagenesis, Site-Directed; Oocytes; Rats; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Reducing Agents; Structure-Activity Relationship; Sulfhydryl Reagents; Xenopus; Zinc | 2002 |
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 |
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 |
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 |
Identification of a region of the ileal-type sodium/bile acid cotransporter interacting with a competitive bile acid transport inhibitor.
Topics: Amino Acid Sequence; Animals; Bile Acids and Salts; Binding, Competitive; Biological Transport, Active; Carrier Proteins; Cell Line; CHO Cells; Cricetinae; Cysteine; Humans; Hydroxysteroid Dehydrogenases; Ileum; Kinetics; Membrane Glycoproteins; Mesylates; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Organic Anion Transporters, Sodium-Dependent; Peptide Fragments; Rats; Recombinant Fusion Proteins; Sequence Alignment; Serine; Symporters; Taurocholic Acid; Thiazepines; Threonine; Valine | 2002 |
Identification of a functionally important conformation-sensitive region of the secretory Na+-K+-2Cl- cotransporter (NKCC1).
Topics: Alanine; Amino Acid Sequence; Animals; Biological Transport; Cell Line; Cysteine; Ethyl Methanesulfonate; Extracellular Space; Humans; Kidney; Mercury; Mesylates; Molecular Sequence Data; Mutagenesis; Protein Conformation; Rats; Rubidium Radioisotopes; Sodium-Potassium-Chloride Symporters; Solute Carrier Family 12, Member 2; Sulfhydryl Reagents | 2003 |
Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel.
Topics: Amino Acid Sequence; Archaea; Base Sequence; Cloning, Molecular; Cysteine; DNA, Complementary; Escherichia coli; Eukaryotic Cells; Evolution, Molecular; Membrane Potentials; Mesylates; Methanococcus; Molecular Sequence Data; Potassium; Potassium Channels, Voltage-Gated; Prokaryotic Cells; Protein Structure, Tertiary; Saccharomyces cerevisiae | 2003 |
Functional characterization of cysteine residues in GlpT, the glycerol 3-phosphate transporter of Escherichia coli.
Topics: 4-Chloromercuribenzenesulfonate; Biological Transport; Cysteine; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Histidine; Immunoblotting; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Proteolipids; Structure-Activity Relationship; Substrate Specificity; Sulfhydryl Reagents | 2003 |
Localization of PIP2 activation gate in inward rectifier K+ channels.
Topics: Amino Acid Sequence; Animals; Cadmium; Cysteine; Ethyl Methanesulfonate; Ion Channel Gating; Mesylates; Molecular Conformation; Molecular Sequence Data; Mutation; Oocytes; Phosphatidylinositol 4,5-Diphosphate; Potassium Channels, Inwardly Rectifying; Protein Structure, Tertiary; Silver; Xenopus laevis | 2003 |
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 |
Structure-function analysis of the bestrophin family of anion channels.
Topics: Amino Acid Sequence; Animals; Anions; Bestrophins; Binding Sites; Cell Line; Cell Membrane; Chloride Channels; Cloning, Molecular; Cysteine; Electrophysiology; Eye Proteins; Genome; Glycosylation; Humans; Ion Channels; Mesylates; Mice; Microscopy, Fluorescence; Models, Biological; Molecular Sequence Data; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oocytes; Phylogeny; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Structure-Activity Relationship; Sulfhydryl Reagents; Time Factors; Transfection; Xenopus | 2003 |
Disulfide bond structure and accessibility of cysteines in the ectodomain of the cholecystokinin receptor: specific mono-reactive receptor constructs examine charge-sensitivity of loop regions.
Topics: Animals; CHO Cells; Cricetinae; Cricetulus; Cysteine; Disulfides; Mesylates; Mutation; Receptors, Cholecystokinin; Serine; Sulfhydryl Reagents | 2003 |
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 |
Creation of a fully functional cysteine-less variant of osmosensor and proton-osmoprotectant symporter ProP from Escherichia coli and its application to assess the transporter's membrane orientation.
Topics: Amino Acid Sequence; Amino Acid Substitution; Carboxylic Acids; Cell Membrane; Cysteine; Escherichia coli Proteins; Fluorescent Dyes; Genetic Variation; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Osmolar Concentration; Osmotic Pressure; Protein Engineering; Protein Transport; Protons; Recombinant Proteins; Symporters | 2003 |
Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis.
Topics: Amino Acid Substitution; Biological Transport; Carrier Proteins; Cysteine; Dipeptides; Ethyl Methanesulfonate; Humans; Membrane Proteins; Mesylates; Mutagenesis, Site-Directed; Peptide Transporter 1; Protein Conformation; Symporters | 2003 |
The orientation and molecular movement of a k(+) channel voltage-sensing domain.
Topics: Animals; Cysteine; Dithiothreitol; Drosophila; Drosophila Proteins; Electric Conductivity; Hydrogen Peroxide; Indicators and Reagents; Membrane Potentials; Mesylates; Models, Biological; Molecular Biology; Mutation; Oocytes; Oxidants; Patch-Clamp Techniques; Potassium Channels; Potassium Channels, Voltage-Gated; Protein Conformation; Protein Structure, Tertiary; Rhodamines; Sequence Alignment; Shaker Superfamily of Potassium Channels; Structure-Activity Relationship; Time Factors; Xenopus laevis | 2003 |
Changes in local S4 environment provide a voltage-sensing mechanism for mammalian hyperpolarization-activated HCN channels.
Topics: Animals; Cell Membrane; Cyclic Nucleotide-Gated Cation Channels; Cysteine; Electrophysiology; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; Ion Channel Gating; Ion Channels; Mammals; Membrane Potentials; Mesylates; Oocytes; Potassium Channels; Potassium Channels, Voltage-Gated; Sulfhydryl Reagents; Xenopus | 2004 |
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 |
The substrate anion selectivity filter in the human erythrocyte Cl-/HCO3- exchange protein, AE1.
Topics: Anion Exchange Protein 1, Erythrocyte; Anions; Cysteine; Erythrocytes; Humans; Mesylates; Mutation; Protein Transport; Substrate Specificity | 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 |
Dynamic membrane topology of the Escherichia coli beta-glucoside transporter BglF.
Topics: Amino Acid Sequence; Carbohydrates; Catalysis; Cell Membrane; Cysteine; Cytoplasm; Escherichia coli; Escherichia coli Proteins; Glucosides; Indicators and Reagents; Ligands; Membrane Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutation; Phosphorylation; Phosphotransferases; Plasmids; Protein Kinases; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Time Factors | 2005 |
Conformationally sensitive residues in extracellular loop 5 of the Na+/dicarboxylate co-transporter.
Topics: Amino Acid Sequence; Animals; Anions; Biological Transport; Biotinylation; Blotting, Western; Cations; Cell Line; Cell Membrane; Cloning, Molecular; Cysteine; Cystine; Dicarboxylic Acid Transporters; Dose-Response Relationship, Drug; Humans; Indicators and Reagents; Inhibitory Concentration 50; Ions; Kinetics; Mesylates; Models, Chemical; Molecular Sequence Data; Mutagenesis; Mutation; Organic Anion Transporters, Sodium-Dependent; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits; Sequence Homology, Amino Acid; Sodium; Symporters; Temperature; Threonine; Time Factors; Valine | 2005 |
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 |
An intersubunit zinc binding site in rat P2X2 receptors.
Topics: Adenosine Triphosphate; Allosteric Site; Animals; Binding Sites; Blotting, Western; Cell Membrane; Cysteine; Dimerization; Disulfides; Dithiothreitol; DNA, Complementary; Dose-Response Relationship, Drug; Histidine; Humans; Ions; Ligands; Mesylates; Models, Biological; Mutagenesis, Site-Directed; Mutation; Oocytes; Protein Binding; Protein Structure, Tertiary; Rats; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Sulfhydryl Reagents; Xenopus; Zinc | 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 |
Roles of transmembrane domain 2 and the first intracellular loop in human noradrenaline transporter function: pharmacological and SCAM analysis.
Topics: Adrenergic Agonists; Amino Acid Motifs; Animals; Binding, Competitive; Brain; Brain Chemistry; Cell Membrane; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Humans; Mesylates; Mutagenesis, Site-Directed; Neurochemistry; Neurons; Neuropharmacology; Norepinephrine; Norepinephrine Plasma Membrane Transport Proteins; Protein Structure, Tertiary; Radioligand Assay; Symporters | 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 |
Functional architecture of the inner pore of a voltage-gated Ca2+ channel.
Topics: Amino Acid Sequence; Animals; Binding Sites; Calcium Channels; Calcium Channels, N-Type; Cells, Cultured; Cloning, Molecular; Cysteine; Ethyl Methanesulfonate; Ion Channel Gating; Membrane Potentials; Mesylates; Models, Molecular; Molecular Sequence Data; Oocytes; Patch-Clamp Techniques; Protein Structure, Quaternary; Sequence Alignment; Structure-Activity Relationship; Sulfhydryl Reagents; Time Factors; Xenopus laevis | 2005 |
Localization of the activation gate of a voltage-gated Ca2+ channel.
Topics: Amino Acid Sequence; Animals; Calcium Channels, N-Type; Cloning, Molecular; Cysteine; Intracellular Membranes; Ion Channel Gating; Membrane Potentials; Mesylates; Molecular Sequence Data; Mutation; Oocytes; Patch-Clamp Techniques; Protein Structure, Secondary; Sequence Alignment; Sulfhydryl Reagents; Time Factors; Xenopus laevis | 2005 |
Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance.
Topics: Amino Acid Transport System X-AG; Animals; Aspartic Acid; Cell Line; Cloning, Molecular; Cysteine; Dose-Response Relationship, Drug; Drug Interactions; Electric Stimulation; Glutamates; Humans; Ion Channel Gating; Lithium; Membrane Potentials; Mesylates; Microinjections; Mutagenesis; Mutation; Neurons; Oocytes; Patch-Clamp Techniques; Protein Conformation; Protein Structure, Tertiary; Sodium; Sulfhydryl Compounds; Transfection; Xenopus | 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 |
Voltage-dependent gating rearrangements in the intracellular T1-T1 interface of a K+ channel.
Topics: Animals; Binding Sites; Cysteine; Dimerization; Kv Channel-Interacting Proteins; Kv1.4 Potassium Channel; Membrane Potentials; Mesylates; Patch-Clamp Techniques; Potassium Channels, Voltage-Gated; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Sulfhydryl Compounds; Xenopus laevis | 2006 |
Conformationally sensitive reactivity to permeant sulfhydryl reagents of cysteine residues engineered into helical hairpin 1 of the glutamate transporter GLT-1.
Topics: Amino Acid Sequence; Biological Transport; Cell Membrane Permeability; Cross-Linking Reagents; Cysteine; Cytoplasm; Ethylmaleimide; Excitatory Amino Acid Transporter 2; HeLa Cells; Humans; Kainic Acid; Mesylates; Molecular Sequence Data; Mutant Proteins; Oxidation-Reduction; Phenanthrolines; Protein Engineering; Protein Structure, Secondary; Protein Structure, Tertiary; Sulfhydryl Reagents | 2007 |
Structural determinants of the closed KCa3.1 channel pore in relation to channel gating: results from a substituted cysteine accessibility analysis.
Topics: Amino Acid Substitution; Animals; Binding Sites; Calcium; Cysteine; Diffusion; Ethyl Methanesulfonate; HeLa Cells; Humans; Hydrophobic and Hydrophilic Interactions; Indicators and Reagents; Intermediate-Conductance Calcium-Activated Potassium Channels; Ion Channel Gating; Mesylates; Models, Chemical; Oocytes; Potassium; Protein Structure, Quaternary; Protein Structure, Tertiary; Structure-Activity Relationship; Xenopus laevis | 2007 |
Cysteine scanning of transmembrane domain three of the human dipeptide transporter: implications for substrate transport.
Topics: Base Sequence; Binding Sites; Biological Transport, Active; Cell Line; Cysteine; Dipeptides; Ethyl Methanesulfonate; Humans; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Transporter 1; Point Mutation; Substrate Specificity; Symporters; Transfection | 2007 |
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 |
Gating the pore of P2X receptor channels.
Topics: Amino Acid Substitution; Animals; Cadmium Compounds; Cell Line; Cell Membrane; Cysteine; Humans; Ion Channel Gating; Kidney; Mesylates; Models, Biological; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Protein Structure, Tertiary; Rats; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Silver Nitrate; Transfection | 2008 |
Identification of conformationally sensitive amino acids in the Na(+)/dicarboxylate symporter (SdcS).
Topics: Amino Acid Sequence; Amino Acid Substitution; Amino Acids; Animals; Bacterial Proteins; Biological Transport; Blotting, Western; Cell Membrane; Cysteine; Kinetics; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutant Proteins; Protein Conformation; Rabbits; Sequence Alignment; Sodium; Staphylococcus aureus; Succinates; Symporters; Time Factors; Transport Vesicles | 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 |
Structural determinants of ion permeation in CRAC channels.
Topics: Amino Acid Sequence; Amino Acid Substitution; Calcium; Calcium Channels; Cysteine; Humans; In Vitro Techniques; Ion Transport; Lanthanum; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; ORAI1 Protein; Protein Structure, Secondary; Recombinant Proteins; Sequence Homology, Amino Acid; Sulfhydryl Reagents | 2009 |
Locale and chemistry of spermine binding in the archetypal inward rectifier Kir2.1.
Topics: Animals; Cell Line; Cysteine; Ethyl Methanesulfonate; Kidney; Macaca mulatta; Mesylates; Models, Molecular; Patch-Clamp Techniques; Potassium Channels, Inwardly Rectifying; Protein Binding; Spermine; Transfection | 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 |
Changes in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel.
Topics: Adenosine Triphosphate; Animals; Cell Line; Cricetinae; Cricetulus; Cyclic AMP-Dependent Protein Kinases; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Cytoplasm; Gold Compounds; Humans; Mesylates; Models, Molecular; Patch-Clamp Techniques; Point Mutation; Protein Conformation; Sulfhydryl Reagents | 2010 |
Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.
Topics: Animals; Cell Membrane Permeability; Chlorides; CHO Cells; Cricetinae; Cricetulus; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Ethyl Methanesulfonate; Ion Channel Gating; Kinetics; Membrane Potentials; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Patch-Clamp Techniques; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Transfection | 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 |
Analysis of the glucagon receptor first extracellular loop by the substituted cysteine accessibility method.
Topics: Amino Acid Sequence; Binding Sites; Cells, Cultured; Cysteine; Glucagon; Humans; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Receptors, Glucagon; Transfection | 2011 |
Functional consequences of sulfhydryl modification of the γ-aminobutyric acid transporter 1 at a single solvent-exposed cysteine residue.
Topics: Animals; Cysteine; Dithiothreitol; Ethylmaleimide; Female; GABA Plasma Membrane Transport Proteins; gamma-Aminobutyric Acid; Gene Expression; Humans; Kinetics; Mesylates; Mutation; Oocytes; Patch-Clamp Techniques; Rhodamines; Sodium Chloride; Sulfhydryl Reagents; Transfection; Valproic Acid; Xenopus laevis | 2012 |
The cardiac Na+-Ca2+ exchanger has two cytoplasmic ion permeation pathways.
Topics: Amino Acid Sequence; Animals; Cysteine; Cytoplasm; Ion Transport; Ions; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutant Proteins; Mutation; Myocardium; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Sodium-Calcium Exchanger; Xenopus | 2013 |
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 |
Comprehensive cysteine-scanning mutagenesis reveals Claudin-2 pore-lining residues with different intrapore locations.
Topics: Amino Acid Sequence; Animals; Claudins; Cysteine; Dogs; Epithelium; Genetic Testing; Madin Darby Canine Kidney Cells; Mesylates; Mice; Molecular Sequence Data; Mutagenesis; Porosity; Protein Structure, Secondary | 2014 |