ethyl methanesulfonate has been researched along with cysteine in 110 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (1.82) | 18.7374 |
| 1990's | 26 (23.64) | 18.2507 |
| 2000's | 68 (61.82) | 29.6817 |
| 2010's | 12 (10.91) | 24.3611 |
| 2020's | 2 (1.82) | 2.80 |
| Authors | Studies |
|---|---|
| Goncharova, RI; Kuzhir, TD | 1 |
| Alam, M; Hartmann, HA; Kirsch, GE | 1 |
| Chen, J; Fu, D; Javitch, JA; Karlin, A | 1 |
| Akabas, MH; Goulding, EH; Karlin, A; Siegelbaum, SA; Sun, ZP | 1 |
| Karlin, A; Kuner, T; Sakmann, B; Seeburg, PH; Wollmuth, LP | 1 |
| Ballesteros, JA; Chen, J; Fu, D; Javitch, JA; Weinstein, H | 1 |
| Chen, J; Fu, D; Javitch, JA | 1 |
| Holmgren, M; Liu, Y; Xu, Y; Yellen, G | 1 |
| Goldstein, SA; Tai, KK; Wang, KW | 1 |
| Chen, S; Hartmann, HA; Kirsch, GE | 1 |
| Chiamvimonvat, N; Marban, E; Pérez-García, MT; Tomaselli, GF | 1 |
| Chen, JG; Liu-Chen, S; Rudnick, G | 1 |
| Janecki, M; Marban, E; Tomaselli, GF; Yamagishi, T | 1 |
| Chen, J; Fu, D; Javitch, JA; Liapakis, G | 1 |
| Chen, JG; Rudnick, G; Sachpatzidis, A | 1 |
| Lo, B; Silverman, M | 1 |
| Egan, TM; Haines, WR; Voigt, MM | 1 |
| Iwaoka, M; Juminaga, D; Scheraga, HA | 1 |
| Karlin, A; Zhang, H | 1 |
| Akabas, MH; Karlin, A | 1 |
| Boileau, AJ; Czajkowski, C; Davis, AF; Evers, AR | 1 |
| Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Simpson, MM | 1 |
| Frang, H; Hoffrén, AM; Javitch, JA; Johnson, MS; Kallio, J; Marjamäki, A; Pihlavisto, M; Salminen, T; Scheinin, M | 1 |
| Lu, T; Yang, J; Zhu, YG | 1 |
| Becchetti, A; Gamel, K; Torre, V | 1 |
| Bucher, DB; Olson, DR; Snyder, PM | 1 |
| Biber, J; Forster, IC; Lambert, G; Murer, H; Stange, G | 1 |
| Bai, G; Chen, HS; Choi, YB; Le, DA; Lipton, SA; Ortiz, J; Tenneti, L | 1 |
| Chen, N; Ferrer, JV; Javitch, JA; Justice, JB | 1 |
| Deng, HB; Guang, W; Wang, JB | 1 |
| Brauer, D; Dean, AM; Kaplan, RS; Kotaria, R; Mayor, JA; Walters, DE | 1 |
| Amara, SG; Leighton, BH; Seal, RP | 1 |
| Cohen, JB; Sullivan, DA | 1 |
| Hill, BJ; Huang, L; Milanick, MA; Parkinson, EL; Wilson, BJ; Xu, W | 1 |
| Biber, J; Forster, IC; Lambert, G; Murer, H | 1 |
| Chen, TY; Lin, CW | 1 |
| Balser, JR; Ong, BH; Tomaselli, GF | 1 |
| Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Xu, W | 1 |
| Karlin, A; Wilson, G | 1 |
| Loussouarn, G; Masia, R; Nichols, CG; Phillips, LR; Rose, T | 1 |
| Beck, C; Kuner, T; Sakmann, B; Seeburg, PH | 1 |
| Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Shi, L; Weinstein, H; Xu, W | 1 |
| Ding, PZ; Wilson, TH | 1 |
| Egan, TM; Haines, WR; Migita, K; Torres, GE; Voigt, MM | 1 |
| O'Reilly, JP; Wang, GK; Wang, SY | 1 |
| Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
| Androutsellis-Theotokis, A; Ghassemi, F; Rudnick, G | 1 |
| Christie, DL; Dodd, JR | 1 |
| Matiach, A; Schröder-Köhne, S | 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 |
| Arrabit, C; Cruz, H; Panicker, S; Slesinger, PA | 1 |
| Bloodworth, LM; Hamdan, FF; Siddiqui, NA; Ward, SD; Wess, J | 1 |
| Giangregorio, N; Iacobazzi, V; Indiveri, C; Palmieri, F | 1 |
| Haddrill, JL; Lynch, JW; Shan, Q | 1 |
| Androutsellis-Theotokis, A; Rudnick, G | 1 |
| Krom, BP; Lolkema, JS | 1 |
| Dehaye, JP; Nagy, A; Premkumar, A; Turner, RJ | 1 |
| Kleyman, TR; Li, J; Perry, CJ; Sheng, S | 1 |
| Flynn, GE; Zagotta, WN | 1 |
| Beaulieu, ME; Boucard, AA; Escher, E; Guillemette, G; Lavigne, P; Leduc, R; Roy, M | 1 |
| Xiao, J; Yang, J; Zhen, XG | 1 |
| ROBERTS, JJ; WARWICK, GP | 1 |
| Haworth, IS; Kulkarni, AA; Lee, VH; Uchiyama, T | 1 |
| Droogmans, G; Janssens, A; Nilius, B; Voets, T | 1 |
| Filippova, N; Weiss, DS; Wotring, VE | 1 |
| Bhogal, N; Blaney, FE; Findlay, JB; Ingley, PM; Rees, J | 1 |
| Guennoun, S; Horisberger, JD; Kharoubi-Hess, S; Michielin, O | 1 |
| Alexeyev, MF; Audia, JP; Daugherty, RM; Roberts, RA; Winkler, HH | 1 |
| Boucard, AA; Clément, M; Escher, E; Guillemette, G; Leduc, R; Martin, SS | 1 |
| Cheetham, SC; Cockcroft, VB; Cox, A; Donnelly, D; Findlay, JB; Kaur, M | 1 |
| Allemann, RK; Daines, AM; Flitsch, SL; Swanwick, RS | 1 |
| Barnett-Norris, J; Hurst, DP; Reggio, PH; Song, ZH; Zhang, R | 1 |
| Rudnick, G; Zhang, YW | 1 |
| Narayan, M; Scheraga, HA; Xu, G | 1 |
| Bryan-Lluka, LJ; Sucic, S | 1 |
| Fitzmaurice, A; Orenstein, ET; Schoonover, CE; Xie, C; Yang, J; Zhen, XG | 1 |
| Beuming, T; Javitch, JA; Sen, N; Shi, L; Weinstein, H | 1 |
| Meijberg, W; Miedema, H; Vrouenraets, M; Wierenga, J | 1 |
| Banerjee, A; Chang, C; Khantwal, CM; Ray, A; Swaan, PW | 1 |
| Kurata, HT; Marton, LJ; Nichols, CG | 1 |
| Banerjee, A; Hussainzada, N; Swaan, PW | 1 |
| Cravatt, BF; Dubin, AE; Evans, MJ; Macpherson, LJ; Marr, F; Patapoutian, A; Schultz, PG | 1 |
| Fu, J; McLaughlin, JT; Rosenberg, RL | 1 |
| Banderali, U; Garneau, L; Klein, H; Parent, L; Sauvé, R; Simoes, M | 1 |
| Escher, E; Guillemette, G; Holleran, BJ; Leduc, R; Martin, SS | 1 |
| Davies, DL; Haworth, IS; Kulkarni, AA; Lee, VH; Links, JL | 1 |
| Bhattacharyya, J; Enkvetchakul, D; Jeliazkova, I; Nichols, CG | 1 |
| Giangregorio, N; Indiveri, C; Palmieri, F; Tonazzi, A | 1 |
| Au, KW; Lau, CP; Li, RA; Siu, CW; Tse, HF | 1 |
| Cui, G; McCarty, NA; O'Brien, AR; Song, B; Zhang, ZR | 1 |
| Liu, T; Lo, B; Silverman, M; Speight, P | 1 |
| Diraviyam, K; Kurata, HT; Marton, LJ; Nichols, CG | 1 |
| Beaulieu, ME; Domazet, I; Escher, E; Guillemette, G; Holleran, BJ; Lavigne, P; Leduc, R; Yan, LP | 1 |
| Allsopp, RC; Evans, RJ; Roberts, JA; Valente, M; Watt, D | 1 |
| Escher, E; Guillemette, G; Holleran, BJ; Lavigne, P; Leduc, R; Yan, L | 1 |
| Chen, TY; Yu, WP; Zhang, XD | 1 |
| Kurata, HT; Nichols, CG; Zhu, EA | 1 |
| Miedema, H; Vrouenraets, M | 1 |
| Bai, Y; Hwang, TC; Li, M | 1 |
| Chu, XP; Inoue, K; Jiang, Q; Papasian, CJ; Wang, JQ; Wu, X; Xiong, ZG | 1 |
| Aguayo, LG; Castro, PA; Figueroa, M; San Martin, LS; Yevenes, GE | 1 |
| Absalom, N; Ambrus, JI; Chebib, M; Halliday, JI; Lin, D; Lochner, M; Lummis, SC; McLeod, MD; Quek, GX; Thompson, AJ | 1 |
| Holmgren, M; Lopez-Rodriguez, A | 1 |
| Boulais, PE; Escher, E; Leduc, R | 1 |
| Boulais, PE; Cabana, J; Escher, E; Holleran, BJ; Lavigne, P; Leduc, R; Sainsily, X | 1 |
| Capobianco, L; Cappello, AR; Curcio, R; Dolce, V; Fiermonte, G; Fiorillo, M; Lauria, G; Lunetti, P; Montalto, A; Muto, L; Onofrio, A; Pierri, CL; Vozza, A | 1 |
| Beard, JM; O'Reilly, JP; Shockett, PE | 1 |
| Deutsch, C; Panyi, G; Papp, F; Szanto, TG; Varga, Z; Zakany, F | 1 |
110 other study(ies) available for ethyl methanesulfonate and cysteine
| Article | Year |
|---|---|
A comparative study of the antimutagenic effects of antioxidants on chemical mutagenesis in Drosophila melanogaster.
Topics: Animals; Antioxidants; Butylated Hydroxytoluene; Cysteamine; Cysteine; Dihydropyridines; Drosophila melanogaster; Ethyl Methanesulfonate; Female; Genes, Dominant; Genes, Lethal; Male; Mutagens; Mutation; Radiation-Protective Agents | 1989 |
Differential effects of sulfhydryl reagents on saxitoxin and tetrodotoxin block of voltage-dependent Na channels.
Topics: Animals; Biophysical Phenomena; Biophysics; Brain; Cysteine; DNA, Complementary; Electrochemistry; Ethyl Methanesulfonate; Female; Humans; In Vitro Techniques; Molecular Conformation; Myocardium; Point Mutation; Saxitoxin; Sodium Channel Blockers; Sodium Channels; Sulfhydryl Reagents; Tetrodotoxin | 1994 |
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 |
Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating.
Topics: Amino Acid Sequence; Animals; Cattle; Cell Membrane Permeability; Chemical Phenomena; Chemistry, Physical; Cyclic Nucleotide-Gated Cation Channels; Cysteine; Ethyl Methanesulfonate; Eye Proteins; Ion Channel Gating; Ion Channels; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Sulfhydryl Reagents | 1996 |
Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines.
Topics: Amino Acid Sequence; Animals; Cysteine; Cytoplasm; Ethyl Methanesulfonate; Extracellular Space; Female; Indicators and Reagents; Ion Channel Gating; Membrane Proteins; Molecular Sequence Data; Mutation; Oocytes; Protein Conformation; Protein Structure, Tertiary; Receptors, N-Methyl-D-Aspartate; Xenopus laevis | 1996 |
Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice.
Topics: Amino Acid Sequence; Binding Sites; Cell Line; Cysteine; Dopamine Antagonists; Ethyl Methanesulfonate; GTP-Binding Proteins; Humans; Kinetics; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Dopamine D2; Signal Transduction; Spiperone; Sulfhydryl Reagents; Sulpiride | 1996 |
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 |
On the use of thiol-modifying agents to determine channel topology.
Topics: Animals; Cell Line; Cell Membrane Permeability; Cysteine; Ethyl Methanesulfonate; Indicators and Reagents; Liposomes; Mutagenesis, Site-Directed; Nitrobenzoates; Oocytes; Patch-Clamp Techniques; Permeability; Potassium Channels; Quaternary Ammonium Compounds; Shaker Superfamily of Potassium Channels; Sulfhydryl Compounds; Xenopus | 1996 |
MinK potassium channels are heteromultimeric complexes.
Topics: Animals; Cysteine; Ethyl Methanesulfonate; Potassium Channel Blockers; Potassium Channels; Potassium Channels, Voltage-Gated; Rats; Recombinant Proteins; Tetraethylammonium; Tetraethylammonium Compounds; Xenopus laevis | 1997 |
Cysteine mapping in the ion selectivity and toxin binding region of the cardiac Na+ channel pore.
Topics: Amino Acid Sequence; Amphibian Proteins; Carrier Proteins; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ion Channel Gating; Molecular Sequence Data; Mutation; Myocardium; Sodium Channels | 1997 |
Control of ion flux and selectivity by negatively charged residues in the outer mouth of rat sodium channels.
Topics: Amino Acids; Animals; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Ion Channel Gating; Mutagenesis; Mutation; Patch-Clamp Techniques; Rats; Sodium Channels; Sulfhydryl Reagents; Xenopus laevis | 1996 |
External cysteine residues in the serotonin transporter.
Topics: Animals; Carrier Proteins; Cysteine; Ethyl Methanesulfonate; HeLa Cells; Humans; Indicators and Reagents; Membrane Glycoproteins; Membrane Transport Proteins; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Rats; Serotonin; Serotonin Plasma Membrane Transport Proteins; Sodium; Transfection | 1997 |
Topology of the P segments in the sodium channel pore revealed by cysteine mutagenesis.
Topics: Amino Acid Sequence; Animals; Cadmium; Calcium Channels; Cell Line; Cell Membrane; Cysteine; Ethyl Methanesulfonate; Kinetics; Membrane Potentials; Models, Structural; Muscle, Skeletal; Mutagenesis, Site-Directed; Point Mutation; Potassium Channels; Protein Structure, Secondary; Rats; Recombinant Proteins; Sequence Alignment; Sodium Channels; Transfection | 1997 |
Constitutive activation of the beta2 adrenergic receptor alters the orientation of its sixth membrane-spanning segment.
Topics: Adrenergic beta-Agonists; Binding Sites; Binding, Competitive; Cell Membrane; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Isoproterenol; Ligands; Propanolamines; Protein Conformation; Receptors, Adrenergic, beta-2 | 1997 |
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 |
Replacement of Ala-166 with cysteine in the high affinity rabbit sodium/glucose transporter alters transport kinetics and allows methanethiosulfonate ethylamine to inhibit transporter function.
Topics: Alanine; Animals; Biological Transport; Cysteine; Ethyl Methanesulfonate; Kinetics; Membrane Glycoproteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Rabbits; Recombinant Proteins; Sodium-Glucose Transporter 1; Xenopus laevis | 1998 |
A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Cells, Cultured; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ion Channel Gating; Kidney; Membrane Potentials; Molecular Sequence Data; Mutagenesis, Site-Directed; Neuropeptides; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Silver; Water | 1998 |
Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease A missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease A and kinetic roles of Cys65 and Cys72.
Topics: Animals; Cattle; Cysteine; Disulfides; Dithiothreitol; Entropy; Ethyl Methanesulfonate; Indicators and Reagents; Kinetics; Models, Chemical; Mutation; Oxidants; Oxidation-Reduction; Protein Folding; Recombinant Proteins; Ribonuclease, Pancreatic | 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 |
Substituted-cysteine accessibility method.
Topics: Amino Acid Substitution; Animals; Binding Sites; Cysteine; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channel Gating; Ion Channels; Kinetics; Mutagenesis, Site-Directed; Protein Structure, Secondary; Recombinant Proteins; Static Electricity; Sulfhydryl Reagents | 1998 |
Mapping the agonist binding site of the GABAA receptor: evidence for a beta-strand.
Topics: Animals; Binding Sites; Biotin; Chromosome Mapping; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; GABA Agonists; gamma-Aminobutyric Acid; Humans; Indicators and Reagents; Kidney; Membrane Potentials; Models, Molecular; Molecular Sequence Data; Muscimol; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Tertiary; Receptors, GABA-A; Sequence Homology, Amino Acid; Tritium; Xenopus | 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 |
Chloroethylclonidine and 2-aminoethyl methanethiosulfonate recognize two different conformations of the human alpha(2A)-adrenergic receptor.
Topics: Adrenergic alpha-Antagonists; Amino Acid Substitution; Animals; Binding Sites; CHO Cells; Clonidine; Cricetinae; Cysteine; Ethyl Methanesulfonate; Humans; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Receptors, Adrenergic, alpha-2; Recombinant Proteins; Thermodynamics; Transfection | 1999 |
Cytoplasmic amino and carboxyl domains form a wide intracellular vestibule in an inwardly rectifying potassium channel.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cysteine; Cytoplasm; Ethyl Methanesulfonate; Indicators and Reagents; Molecular Sequence Data; Mutagenesis, Site-Directed; Potassium Channels; Potassium Channels, Inwardly Rectifying; Structure-Activity Relationship; Xenopus | 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 |
A pore segment in DEG/ENaC Na(+) channels.
Topics: Amino Acid Sequence; Cysteine; Epithelial Sodium Channels; Ethyl Methanesulfonate; Humans; Molecular Sequence Data; Mutation; Sequence Homology, Amino Acid; Sodium Channels | 1999 |
Properties of the mutant Ser-460-Cys implicate this site in a functionally important region of the type IIa Na(+)/P(i) cotransporter protein.
Topics: Alkylation; Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channel Gating; Kinetics; Membrane Potentials; Molecular Sequence Data; Mutagenesis; Oocytes; Phosphates; Protein Structure, Tertiary; Rats; RNA, Complementary; Serine; Sodium; Sodium-Phosphate Cotransporter Proteins; Sodium-Phosphate Cotransporter Proteins, Type IIa; Structure-Activity Relationship; Symporters; 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 |
Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter.
Topics: Biological Transport; Carrier Proteins; Cell Line; Cocaine; Cysteine; Cytoplasm; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Inhibitory Concentration 50; Kinetics; Membrane Glycoproteins; Membrane Transport Proteins; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Binding; Protein Conformation; Temperature; Time Factors; Tyramine | 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 |
A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines.
Topics: Amino Acid Sequence; Amino Acid Transport System X-AG; Amino Acids; Animals; ATP-Binding Cassette Transporters; Biotin; COS Cells; Cysteine; Ethyl Methanesulfonate; Extracellular Space; Humans; Indicators and Reagents; Ion Channel Gating; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Tertiary | 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 |
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 |
Cysteine modification of a putative pore residue in ClC-0: implication for the pore stoichiometry of ClC chloride channels.
Topics: Animals; Chloride Channels; Chlorides; Cysteine; Dimerization; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channel Gating; Mutagenesis, Site-Directed; Xenopus | 2000 |
A structural rearrangement in the sodium channel pore linked to slow inactivation and use dependence.
Topics: Anesthetics, Local; Animals; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Indicators and Reagents; Kinetics; Lidocaine; Membrane Potentials; Muscle, Skeletal; Mutagenesis, Site-Directed; Rats; Sodium Channels | 2000 |
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 |
Acetylcholine receptor channel structure in the resting, open, and desensitized states probed with the substituted-cysteine-accessibility method.
Topics: Acetylcholine; Amino Acid Substitution; Animals; Cysteine; Ethyl Methanesulfonate; In Vitro Techniques; Ion Channel Gating; Lidocaine; Membrane Potentials; Mice; Models, Molecular; Muscle, Skeletal; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Secondary; Protein Subunits; Receptors, Cholinergic; Recombinant Proteins; Xenopus | 2001 |
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 |
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 |
Comparison of the amino acid residues in the sixth transmembrane domains accessible in the binding-site crevices of mu, delta, and kappa opioid receptors.
Topics: Amino Acid Substitution; Amino Acids; Animals; Binding, Competitive; Cysteine; Diprenorphine; Ethyl Methanesulfonate; Humans; Naloxone; Narcotic Antagonists; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Receptors, Opioid; Receptors, Opioid, delta; Receptors, Opioid, kappa; Receptors, Opioid, mu | 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 |
On the contribution of the first transmembrane domain to whole-cell current through an ATP-gated ionotropic P2X receptor.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Cell Line; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Ion Channel Gating; Kidney; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Protein Structure, Tertiary; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Silver; Structure-Activity Relationship; Transfection | 2001 |
Residue-specific effects on slow inactivation at V787 in D2-S6 of Na(v)1.4 sodium channels.
Topics: Amino Acid Motifs; Amino Acid Substitution; Animals; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Ion Channel Gating; Lysine; Membrane Potentials; Models, Biological; Muscle, Skeletal; Patch-Clamp Techniques; Protein Structure, Tertiary; Rats; Sodium Channels | 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 |
A conformationally sensitive residue on the cytoplasmic surface of serotonin transporter.
Topics: Animals; Carrier Proteins; Cysteine; Cytoplasm; Ethyl Methanesulfonate; Ligands; Membrane Glycoproteins; Membrane Transport Proteins; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Binding; Protein Conformation; Rats; Serotonin Plasma Membrane Transport Proteins | 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 |
Yeast cys3 and gsh1 mutant cells display overlapping but non-identical symptoms of oxidative stress with regard to subcellular protein localization and CDP-DAG metabolism.
Topics: Cell Division; Cystathionine gamma-Lyase; Cysteine; Cytidine Diphosphate Diglycerides; DNA-Binding Proteins; Ethyl Methanesulfonate; Fluorescent Antibody Technique, Indirect; Fungal Proteins; Genes, Fungal; Glutamate-Cysteine Ligase; Glutathione; Homeodomain Proteins; Hot Temperature; Lipid Metabolism; Membrane Proteins; Mutagenesis; Mutation; Oxidative Stress; Phenotype; Protein Transport; Recombination, Genetic; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Subcellular Fractions; Transcription Factors; Vesicular Transport Proteins | 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 |
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 |
Use of an in situ disulfide cross-linking strategy to map proximities between amino acid residues in transmembrane domains I and VII of the M3 muscarinic acetylcholine receptor.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; COS Cells; Cross-Linking Reagents; Cysteine; Disulfides; Ethyl Methanesulfonate; Hydrolysis; Ligands; Molecular Sequence Data; Muscarinic Agonists; Muscarinic Antagonists; Mutagenesis, Site-Directed; N-Methylscopolamine; Peptide Fragments; Peptide Mapping; Phosphatidylinositols; Protein Structure, Tertiary; Rats; Receptor, Muscarinic M3; Receptors, Muscarinic; Sulfhydryl Compounds; Transfection; Tritium | 2002 |
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 |
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 |
Conserved residues R420 and Q428 in a cytoplasmic loop of the citrate/malate transporter CimH of Bacillus subtilis are accessible from the external face of the membrane.
Topics: Arginine; Bacillus subtilis; Bacterial Proteins; Calcium; Carrier Proteins; Cell Membrane; Cell Membrane Permeability; Citric Acid; Conserved Sequence; Cysteine; Cytoplasm; Ethyl Methanesulfonate; Ethylmaleimide; Glutamine; Hydroxy Acids; Lysine; Malates; Mutagenesis, Site-Directed; Organic Anion Transporters; Plasmids; Substrate Specificity | 2003 |
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 |
Asymmetric organization of the pore region of the epithelial sodium channel.
Topics: Amiloride; Amino Acid Sequence; Animals; Binding Sites; Cations; Cysteine; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; Epithelial Sodium Channels; Ethyl Methanesulfonate; Indicators and Reagents; Kinetics; Lithium; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Potassium; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine; Sodium; Sodium Channels; Time Factors; Xenopus | 2003 |
A cysteine scan of the inner vestibule of cyclic nucleotide-gated channels reveals architecture and rearrangement of the pore.
Topics: Amino Acid Sequence; Cyclic AMP; Cyclic Nucleotide-Gated Cation Channels; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ion Channel Gating; Ion Channels; Molecular Sequence Data; Oocytes; Patch-Clamp Techniques; Permeability; Point Mutation; Protein Structure, Secondary | 2003 |
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 |
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 |
Mode of action of alkylating agents: formation of S-ethylcysteine from ethyl methanesulphonate in vivo.
Topics: Alkylating Agents; Antineoplastic Agents; Cysteine; Ethyl Methanesulfonate; Humans; Neoplasms | 1957 |
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 |
Outer pore architecture of a Ca2+-selective TRP channel.
Topics: Amino Acid Sequence; Animals; Bacterial Proteins; Calcium; Calcium Channels; Carbon; Cations; Cell Line; Cysteine; DNA; Drosophila; Electrophysiology; Ethyl Methanesulfonate; Genetic Vectors; Humans; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Potassium; Potassium Channels; Protein Conformation; Silver; Sodium; Time Factors; TRPV Cation Channels | 2004 |
Evidence that the TM1-TM2 loop contributes to the rho1 GABA receptor pore.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Cadmium; Cysteine; Ethyl Methanesulfonate; Female; gamma-Aminobutyric Acid; Membrane Potentials; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Polymerase Chain Reaction; Receptors, GABA; Recombinant Proteins; Transfection; Xenopus laevis | 2004 |
Evidence for the proximity of the extreme N-terminus of the neurokinin-2 (NK2) tachykinin receptor to Cys167 in the putative fourth transmembrane helix.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Benzamides; Binding Sites; Binding, Competitive; CHO Cells; Cricetinae; Cysteine; Ethyl Methanesulfonate; Extracellular Space; Glutamic Acid; Humans; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Piperidines; Protein Structure, Secondary; Receptors, Neurokinin-2; Static Electricity; Sulfhydryl Reagents; Tritium | 2004 |
The fourth transmembrane segment of the Na,K-ATPase alpha subunit: a systematic mutagenesis study.
Topics: Acrylamides; Amino Acid Sequence; Animals; Bufo marinus; Cnidarian Venoms; Cysteine; Ethyl Methanesulfonate; Female; Membrane Potentials; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Structure, Secondary; Protein Subunits; Sequence Alignment; Sodium-Potassium-Exchanging ATPase; Sulfhydryl Reagents; Xenopus laevis | 2004 |
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 |
Analysis of the third transmembrane domain of the human type 1 angiotensin II receptor by cysteine scanning mutagenesis.
Topics: Amino Acid Sequence; Animals; Binding Sites; COS Cells; Cysteine; DNA, Complementary; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Isoleucine; Kinetics; Ligands; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptor, Angiotensin, Type 1; Tyrosine | 2004 |
MTSEA prevents ligand binding to the human melanocortin-4 receptor by modification of cysteine 130 in transmembrane helix 3.
Topics: Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Cysteine; Ethyl Methanesulfonate; Humans; Ligands; Models, Molecular; Molecular Sequence Data; Mutation; Protein Structure, Secondary; Receptor, Melanocortin, Type 4 | 2005 |
Synthesis of homogenous site-selectively glycosylated proteins.
Topics: Carbohydrates; Cysteine; Escherichia coli; Ethyl Methanesulfonate; Glycoproteins; Glycosylation; Molecular Structure; Mutagenesis, Site-Directed; Peptide Fragments; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tetrahydrofolate Dehydrogenase | 2005 |
Cysteine 2.59(89) in the second transmembrane domain of human CB2 receptor is accessible within the ligand binding crevice: evidence for possible CB2 deviation from a rhodopsin template.
Topics: Amino Acid Sequence; Binding, Competitive; Cannabinoids; Cell Line; Cell Membrane; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Secondary; Receptor, Cannabinoid, CB2; Rhodopsin | 2005 |
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 |
The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide.
Topics: Animals; Cattle; Chromatography, High Pressure Liquid; Cysteine; Disulfides; Ethyl Methanesulfonate; Isoenzymes; Oligosaccharides; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Fusion Proteins; Ribonuclease, Pancreatic; Structure-Activity Relationship; Thermodynamics | 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 |
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 |
A pincer-like configuration of TM2 in the human dopamine transporter is responsible for indirect effects on cocaine binding.
Topics: Analysis of Variance; Binding Sites; Biotinylation; Blotting, Western; Cell Line; Cell Membrane; Cocaine; Cysteine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Drug Interactions; Ethyl Methanesulfonate; Humans; Imaging, Three-Dimensional; Mercuric Chloride; Mutagenesis; Protein Binding; Protein Structure, Tertiary; Sequence Alignment; Transfection; Tritium; Tropanes; Tyramine | 2005 |
Chemical modification of the bacterial porin OmpF: gain of selectivity by volume reduction.
Topics: Amino Acids; Cysteine; Electrophysiology; Escherichia coli; Ethyl Methanesulfonate; Glutathione; Ion Channel Gating; Mutation; Peptides; Porins; Sensitivity and Specificity | 2006 |
Design of novel synthetic MTS conjugates of bile acids for site-directed sulfhydryl labeling of cysteine residues in bile acid binding and transporting proteins.
Topics: Amino Acid Substitution; Animals; Bile Acids and Salts; Biological Transport; Carrier Proteins; Chlorocebus aethiops; COS Cells; Cysteine; Drug Design; Ethyl Methanesulfonate; Humans; Membrane Glycoproteins; Organic Anion Transporters, Sodium-Dependent; Structure-Activity Relationship; Symporters; Taurocholic Acid | 2006 |
The polyamine binding site in inward rectifier K+ channels.
Topics: Animals; Binding Sites; Biogenic Polyamines; Cell Line; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Membrane Potentials; Models, Biological; Patch-Clamp Techniques; Polyamines; Potassium Channels, Inwardly Rectifying; Protein Binding; Putrescine; Spermine | 2006 |
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 |
Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines.
Topics: Acrolein; Animals; Cysteine; Disulfides; Dithiothreitol; Electric Conductivity; Ethyl Methanesulfonate; Humans; Ion Channel Gating; Mice; Mustard Plant; Noxae; Pain; Plant Oils; Transient Receptor Potential Channels | 2007 |
Agonist-driven conformational changes in the inner beta-sheet of alpha7 nicotinic receptors.
Topics: Acetylcholine; alpha7 Nicotinic Acetylcholine Receptor; Amino Acid Sequence; Amino Acid Substitution; Animals; Chickens; Cysteine; Ethyl Methanesulfonate; Molecular Sequence Data; Mutant Proteins; Protein Structure, Secondary; Receptors, Nicotinic; Xenopus | 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 |
Activation of the angiotensin II type 1 receptor leads to movement of the sixth transmembrane domain: analysis by the substituted cysteine accessibility method.
Topics: Amino Acid Sequence; Animals; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Humans; Molecular Sequence Data; Protein Structure, Tertiary; Receptor, Angiotensin, Type 1 | 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 |
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 |
Structural and functional determinants in the S5-P region of HCN-encoded pacemaker channels revealed by cysteine-scanning substitutions.
Topics: Amino Acid Sequence; Animals; Cadmium Chloride; Cyclic Nucleotide-Gated Cation Channels; Cysteine; Dithiothreitol; Ethyl Methanesulfonate; Female; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; Ion Channel Gating; Kinetics; Membrane Potentials; Mice; Microinjections; Models, Molecular; Molecular Sequence Data; Mutation; Oocytes; Permeability; Potassium Channels; Protein Conformation; Protein Structure, Tertiary; Reducing Agents; Structure-Activity Relationship; Sulfhydryl Compounds; Sulfhydryl Reagents; Xenopus laevis | 2008 |
Mutations at arginine 352 alter the pore architecture of CFTR.
Topics: Amino Acid Substitution; Animals; Arginine; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Drug Stability; Electrophysiology; Ethyl Methanesulfonate; Female; Glipizide; Humans; In Vitro Techniques; Ion Channel Gating; Molecular Structure; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Point Mutation; Recombinant Proteins; Xenopus laevis | 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 |
Blocker protection by short spermine analogs: refined mapping of the spermine binding site in a Kir channel.
Topics: Animals; Binding Sites; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Models, Biological; Potassium Channel Blockers; Potassium Channels, Inwardly Rectifying; Protein Structure, Secondary; Spermine; Time Factors | 2008 |
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 |
Contribution of the region Glu181 to Val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis.
Topics: Adenosine Triphosphate; Affinity Labels; Animals; Azides; Biotinylation; Blotting, Western; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Conformation; Purinergic P2 Receptor Agonists; Receptors, Purinergic P2; Receptors, Purinergic P2X; Xenopus laevis | 2009 |
Analysis of transmembrane domains 1 and 4 of the human angiotensin II AT1 receptor by cysteine-scanning mutagenesis.
Topics: Angiotensin II; Animals; Arginine; Binding Sites; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Membrane Proteins; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Receptor, Angiotensin, Type 1 | 2010 |
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 |
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 |
The ionization state of D37 in E. coli porin OmpF and the nature of conductance fluctuations in D37 mutants.
Topics: Amino Acid Substitution; Arginine; Aspartic Acid; Cations; Cysteine; Electric Conductivity; Electrophysiology; Escherichia coli; Ethyl Methanesulfonate; Hydrogen-Ion Concentration; Ion Channel Gating; Mutation; Porins; Protein Conformation; Time Factors | 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 |
Cysteine 149 in the extracellular finger domain of acid-sensing ion channel 1b subunit is critical for zinc-mediated inhibition.
Topics: Acid Sensing Ion Channels; Analysis of Variance; Animals; Calcium; Cell Line, Transformed; Cricetinae; Cricetulus; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Extracellular Fluid; Hydrogen Peroxide; Membrane Potentials; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Patch-Clamp Techniques; Protein Structure, Tertiary; Rats; Sodium Channels; Trace Elements; Transfection; Zinc | 2011 |
The basic property of Lys385 is important for potentiation of the human α1 glycine receptor by ethanol.
Topics: Amino Acid Substitution; Cell Membrane; Chemical Phenomena; Cysteine; Dose-Response Relationship, Drug; Drug Synergism; Electrophysiological Phenomena; Ethanol; Ethyl Methanesulfonate; Glycine; GTP-Binding Protein beta Subunits; GTP-Binding Protein gamma Subunits; Guanosine 5'-O-(3-Thiotriphosphate); HEK293 Cells; Humans; Ion Channel Gating; Lysine; Models, Molecular; Neurotransmitter Agents; Patch-Clamp Techniques; Propofol; Protein Interaction Domains and Motifs; Receptors, Glycine; Recombinant Fusion Proteins; Static Electricity; Surface Properties; Transfection | 2012 |
Identifying the binding site of novel methyllycaconitine (MLA) analogs at α4β2 nicotinic acetylcholine receptors.
Topics: Aconitine; alpha7 Nicotinic Acetylcholine Receptor; Amino Acid Substitution; Animals; Binding Sites; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Female; Membrane Potentials; Models, Chemical; Models, Molecular; Molecular Structure; Mustard Compounds; Mutagenesis, Site-Directed; Oocytes; Protein Binding; Protein Conformation; Rats; Receptors, Nicotinic; Recombinant Proteins; Structure-Activity Relationship; Xenopus | 2010 |
Restoration of proper trafficking to the cell surface for membrane proteins harboring cysteine mutations.
Topics: Amino Acid Substitution; Animals; Cattle; Cell Membrane; Cyclic Nucleotide-Gated Cation Channels; Cysteine; Ethyl Methanesulfonate; Green Fluorescent Proteins; Humans; Membrane Proteins; Mutant Proteins; Mutation; Recombinant Fusion Proteins; Time Factors; Xenopus | 2012 |
Analysis by substituted cysteine scanning mutagenesis of the fourth transmembrane domain of the CXCR4 receptor in its inactive and active state.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Anti-HIV Agents; Binding Sites; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Receptors, CXCR4 | 2013 |
Identification of transmembrane domain 3, 4 & 5 residues that contribute to the formation of the ligand-binding pocket of the urotensin-II receptor.
Topics: Amino Acid Substitution; Animals; Binding Sites; Cell Culture Techniques; Chlorocebus aethiops; COS Cells; Cysteine; Ethyl Methanesulfonate; Ligands; Models, Molecular; Mutation; Rats; Receptors, G-Protein-Coupled; Transfection; Urotensins | 2013 |
New insights about the structural rearrangements required for substrate translocation in the bovine mitochondrial oxoglutarate carrier.
Topics: Animals; Arginine; Binding Sites; Cattle; Cysteine; Ethyl Methanesulfonate; Gene Expression; Ketoglutaric Acids; Kinetics; Lysine; Membrane Transport Proteins; Mitochondria; Mitochondrial ADP, ATP Translocases; Molecular Docking Simulation; Mutagenesis, Site-Directed; Protein Binding; Protein Domains; Protein Structure, Secondary; Structural Homology, Protein; Substrate Specificity | 2016 |
Substituted cysteine scanning in D1-S6 of the sodium channel hNav1.4 alters kinetics and structural interactions of slow inactivation.
Topics: Amino Acid Substitution; Cysteine; Ethyl Methanesulfonate; HEK293 Cells; Humans; Ion Channel Gating; Molecular Dynamics Simulation; NAV1.4 Voltage-Gated Sodium Channel; Protein Binding; Protein Domains | 2020 |
Molecular rearrangements in S6 during slow inactivation in Shaker-IR potassium channels.
Topics: Cysteine; Ethyl Methanesulfonate; Potassium; Potassium Channels, Voltage-Gated; Shaker Superfamily of Potassium Channels | 2023 |