cysteine has been researched along with methanethiosulfonate in 89 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 21 (23.60) | 18.2507 |
2000's | 52 (58.43) | 29.6817 |
2010's | 16 (17.98) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
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Akabas, MH; Archdeacon, P; Karlin, A; Kaufmann, C | 1 |
Chen, J; Fu, D; Javitch, JA; Karlin, A | 1 |
Brown, AM; Kirsch, GE; Pascual, JM; Shieh, CC | 1 |
Karlin, A; Stauffer, DA | 1 |
Akabas, MH; Cheung, M | 2 |
Chen, J; Fu, D; Javitch, JA | 1 |
Howells, RD; Shahrestanifar, MS | 1 |
Fetrow, JS; Qu, K; Scholes, CP; Sienkiewicz, A; Vaughn, JL | 1 |
Cao, Z; Feix, JB; Foster, SB; Jiang, X; Klebba, PE; Newton, SM; Payne, MA | 1 |
Buell, G; Newbolt, A; North, RA; Rassendren, F; Surprenant, A | 1 |
Feix, JB; Klug, CS; Su, W | 1 |
Grunewald, M; Kanner, BI; Kavanaugh, MP; Zarbiv, R | 1 |
Ferrer, JV; Javitch, JA | 1 |
Jones, LR; Karim, CB; Karim, J; Stamm, JD; Thomas, DD | 1 |
Karlin, A; Pascual, JM | 1 |
Jones, JB; Khumtaveeporn, K; Plettner, E; Shang, X | 1 |
Kriegler, S; Sudweeks, S; Yakel, JL | 1 |
Hu, LA; King, SC | 1 |
Adams, CM; Snyder, PM; Welsh, MJ | 1 |
Akabas, MH; Williams, DB | 1 |
Hubbell, WL; Khorana, HG; Mollaaghababa, R; Steinhoff, HJ | 1 |
Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Shi, L; Simpson, MM; Visiers, I; Weinstein, H | 1 |
Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Xu, W | 1 |
Chen, HV; Choi, Y; Lipton, SA | 1 |
Loussouarn, G; Masia, R; Nichols, CG; Phillips, LR; Rose, T | 1 |
Clarke, DM; Loo, TW | 1 |
Batiza, A; Kung, C; Yoshimura, K | 1 |
Berfield, JL; Ferrer, JV; Javitch, JA; Reith, ME; Wang, LC | 1 |
Fu, J; Kirk, KL | 1 |
Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
Christie, DL; Dodd, JR | 2 |
Blair, DF; Braun, TF | 1 |
Cafiso, DS; Ferguson, CG; Prestwich, GD; Rauch, ME | 1 |
Guennoun, S; Horisberger, JD | 1 |
Lamb, RA; Pinto, LH; Tang, Y; Zaitseva, F | 1 |
Guan, L; Hideg, K; Kaback, HR; Kálai, T; Sahin-Tóth, M | 1 |
Rooney, L; Sobolevsky, AI; Wollmuth, LP | 1 |
Bailey, RJ; Jiang, LH; North, RA; Spelta, V; Surprenant, A | 1 |
Bartlett, MC; Clarke, DM; Loo, TW | 3 |
Beaulieu, ME; Boucard, AA; Escher, E; Guillemette, G; Lavigne, P; Leduc, R; Roy, M | 1 |
O'Reilly, JP; Wang, GK; Wang, SY | 1 |
Chen, TY; Lin, CW | 1 |
Lolkema, JS; Sobczak, I | 1 |
Sobolevsky, AI; Wollmuth, LP; Yelshansky, MV | 1 |
Dimroth, P; Pos, KM; Wild, MR | 1 |
Duell, K; Konopka, JB; Lin, JC | 1 |
Conklin, D; Landfear, SM; Valdés, R; Vasudevan, G | 1 |
Harris, RA; Lobo, IA; Mascia, MP; Trudell, JR | 1 |
Alexeyev, MF; Audia, JP; Daugherty, RM; Roberts, RA; Winkler, HH | 1 |
Capobianco, L; Ferramosca, A; Impagnatiello, T; Zara, V | 1 |
Bacconi, A; Biber, J; Ehnes, C; Forster, IC; Kohler, K; Murer, H; Stange, G | 1 |
Bacconi, A; Biber, J; Ehnes, C; Forster, IC; Kohler, K; Murer, H | 1 |
Gautschi, I; Kellenberger, S; Pfister, Y; Schild, L | 1 |
Fahlke, C; Hebeisen, S | 1 |
Schuldiner, S; Sharoni, M; Steiner-Mordoch, S | 1 |
Audia, JP; Roberts, RA; Winkler, HH | 1 |
Forster, IC; Murer, H; Virkki, LV | 1 |
Altenbach, C; Hideg, K; Hubbell, WL; Phillips, M; Reisler, E; Rubenstein, PA; Shvetsov, A; Stamm, JD; Warshaviak, D | 1 |
Palmer, LG; Sackin, H; Zhang, YY | 1 |
Banerjee, A; Hussainzada, N; Swaan, PW | 1 |
Bevensee, MO; McAlear, SD | 1 |
Carland, JE; Cooper, MA; Deeb, TZ; Hales, TG; Lambert, JJ; Livesey, MR; Peters, JA | 1 |
Bruns, JB; Hughey, RP; Kleyman, TR; Maarouf, AB; Sheng, S | 1 |
Kubo, Y; Nakajo, K | 1 |
Baldwin, SA; Cass, CE; Karpinski, E; Lin, CC; Ng, AM; Slugoski, MD; Smith, KM; Yao, SY; Young, JD; Zhang, J | 1 |
Fillingame, RH; Steed, PR | 1 |
Czajkowski, C; Hanson, SM | 1 |
Digby, HR; El Ajouz, S; Evans, RJ; Kara, M; Roberts, JA; Sutcliffe, MJ | 1 |
Chowdhury, R; Flashman, E; Mecinović, J; Schofield, CJ | 1 |
Chen, TY; Yu, WP; Zhang, XD | 1 |
Nishiya, T; Uehara, T | 1 |
Abramson, J; Chaptal, V; Guan, L; Kaback, HR; Kwon, S; Sawaya, MR | 1 |
El Hiani, Y; Linsdell, P; Wang, W | 1 |
Cunningham, FK; Hammond, JR; Hughes, SJ; Park, JS | 1 |
El Hiani, Y; Linsdell, P; Qian, F | 1 |
El Hiani, Y; Linsdell, P | 1 |
Bai, Y; Gao, X; Hwang, TC | 1 |
Galluccio, M; Hedfalk, K; Indiveri, C; Pingitore, P; Pochini, L; Scalise, M | 1 |
Borghese, CM; Harris, RA; Hicks, JA; Lapid, DJ; Trudell, JR | 1 |
Boucher, A; Jinadasa, T; Josephson, CB; Orlowski, J | 1 |
Brown, LS; Caporini, MA; Good, DB; Ladizhansky, V; Ljumovic, M; Marek, A; Milikisiyants, S; Munro, RA; Rosay, M; Smirnov, AI; Voinov, MA; Ward, ME | 1 |
Binder, BP; James, ZM; McCaffrey, JE; Svensson, B; Thomas, DD | 1 |
Mindell, JA; Mulligan, C | 1 |
Brockwell, DJ; Calabrese, AN; Horne, JE; Kapur, N; Levenstein, MA; Radford, SE; Walko, M; Wilson, AJ | 1 |
Barth, K; Cafiso, DS; Jaumann, EA; Joseph, B; Prisner, TF; Sikora, A | 1 |
1 review(s) available for cysteine and methanethiosulfonate
Article | Year |
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Screening systems for the identification of S-nitrosylated proteins.
Topics: Binding Sites; Biotin; Computational Biology; Cysteine; Disulfides; Mesylates; Nitric Oxide; Oxidation-Reduction; Protein Array Analysis; Protein Processing, Post-Translational; Proteins; Proteomics; S-Nitrosothiols; Substrate Specificity | 2011 |
88 other study(ies) available for cysteine and methanethiosulfonate
Article | Year |
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Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit.
Topics: Acetylcholine; Animals; Cell Membrane; Cysteine; Cytoplasm; Ion Channels; Mesylates; Mice; Models, Molecular; Mutagenesis, Site-Directed; Protein Structure, Secondary; Receptors, Cholinergic; Receptors, Nicotinic; Structure-Activity Relationship; Sulfhydryl Reagents | 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 |
K+ pore structure revealed by reporter cysteines at inner and outer surfaces.
Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cysteine; Electric Conductivity; Female; Gene Expression; Macromolecular Substances; Mesylates; Molecular Sequence Data; Mutagenesis; Oocytes; Polymerase Chain Reaction; Potassium Channels; Recombinant Proteins; RNA, Complementary; Structure-Activity Relationship; Tetraethylammonium; Tetraethylammonium Compounds; Xenopus | 1995 |
Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates.
Topics: Acetylcholine; Animals; Binding Sites; Cysteine; Electrochemistry; In Vitro Techniques; Indicators and Reagents; Mesylates; Models, Chemical; Receptors, Nicotinic; Sulfhydryl Compounds; Torpedo | 1994 |
Identification of cystic fibrosis transmembrane conductance regulator channel-lining residues in and flanking the M6 membrane-spanning segment.
Topics: Amino Acid Sequence; Animals; ATP-Binding Cassette Transporters; Binding Sites; Biophysical Phenomena; Biophysics; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Female; Humans; In Vitro Techniques; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Secondary; Sulfhydryl Reagents; Water; Xenopus laevis | 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 |
Sensitivity of opioid receptor binding to N-substituted maleimides and methanethiosulfonate derivatives.
Topics: Benzomorphans; Binding, Competitive; Cell Line; Cysteine; Humans; Kidney; Kinetics; Maleimides; Mesylates; Mutagenesis, Site-Directed; Narcotic Antagonists; Receptors, Opioid, delta; Receptors, Opioid, mu; Recombinant Proteins; Structure-Activity Relationship; Transfection | 1996 |
Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102.
Topics: Circular Dichroism; Cysteine; Cytochrome c Group; Cytochromes c; Electron Spin Resonance Spectroscopy; Guanidine; Guanidines; Hydrogen-Ion Concentration; Kinetics; Mesylates; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry; Spin Labels; Temperature; Thermodynamics | 1997 |
Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel.
Topics: Anions; Chloride Channels; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Electrophysiology; Humans; Indicators and Reagents; Ion Channel Gating; Kinetics; Mesylates; Mutagenesis; Oligonucleotides; Oocytes; RNA, Messenger; Sulfhydryl Reagents | 1997 |
Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria.
Topics: Bacterial Outer Membrane Proteins; Bacterial Proteins; Biological Transport; Carrier Proteins; Colicins; Cyclic N-Oxides; Cysteine; Electron Spin Resonance Spectroscopy; Enterobactin; Escherichia coli; Escherichia coli Proteins; Ferric Compounds; Indicators and Reagents; Ion Channel Gating; Ligands; Membrane Proteins; Mesylates; Porins; Protein Conformation; Receptors, Cell Surface; Spin Labels | 1997 |
Identification of amino acid residues contributing to the pore of a P2X receptor.
Topics: Adenosine Triphosphate; Binding Sites; Cell Line; Cysteine; Electrophysiology; Ethylamines; Humans; Ion Channel Gating; Ion Channels; Mesylates; Mutagenesis; Quaternary Ammonium Compounds; Receptors, Purinergic P2; Receptors, Purinergic P2X2 | 1997 |
Mapping of the residues involved in a proposed beta-strand located in the ferric enterobactin receptor FepA using site-directed spin-labeling.
Topics: Amino Acid Sequence; Amino Acid Substitution; Bacterial Outer Membrane Proteins; Binding Sites; Carrier Proteins; Colicins; Cysteine; Edetic Acid; Electron Spin Resonance Spectroscopy; Enterobactin; Escherichia coli; Hydroxybutyrates; Lipid Bilayers; Liposomes; Mesylates; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Nickel; Oxalates; Oxygen; Pentanones; Protein Structure, Secondary; Receptors, Cell Surface; Recombinant Proteins; Spin Labels | 1997 |
Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue.
Topics: Amino Acid Transport System X-AG; Amino Acids; Aspartic Acid; ATP-Binding Cassette Transporters; Binding Sites; Biological Transport; Conserved Sequence; Cysteine; Ethylmaleimide; HeLa Cells; Humans; Kainic Acid; Mesylates; Mutagenesis, Site-Directed; Potassium; Protein Conformation; Sodium; Sulfhydryl Reagents | 1998 |
Cocaine alters the accessibility of endogenous cysteines in putative extracellular and intracellular loops of the human dopamine transporter.
Topics: Carrier Proteins; Cell Line; Cocaine; Cysteine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Humans; Kinetics; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Tritium | 1998 |
Cysteine reactivity and oligomeric structures of phospholamban and its mutants.
Topics: Animals; Calcium-Binding Proteins; Calcium-Transporting ATPases; Cysteine; Dithionitrobenzoic Acid; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Isoleucine; Leucine; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Spin Labels; Spodoptera; Sulfhydryl Compounds | 1998 |
Delimiting the binding site for quaternary ammonium lidocaine derivatives in the acetylcholine receptor channel.
Topics: Amino Acid Sequence; Anesthetics, Local; Animals; Binding Sites; Cysteine; Cytoplasm; Electrophysiology; Indicators and Reagents; Ion Channel Gating; Kinetics; Lidocaine; Mesylates; Mice; Molecular Sequence Data; Muscle, Skeletal; Mutagenesis, Site-Directed; Oocytes; Protein Conformation; Receptors, Cholinergic; Xenopus | 1998 |
A combinatorial approach to chemical modification of subtilisin Bacillus lentus.
Topics: Amino Acid Substitution; Bacillus; Cysteine; Drug Design; Indicators and Reagents; Kinetics; Mesylates; Mutagenesis, Site-Directed; Point Mutation; Structure-Activity Relationship; Subtilisins | 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 |
Identification of the amine-polyamine-choline transporter superfamily 'consensus amphipathic region' as the target for inactivation of the Escherichia coli GABA transporter GabP by thiol modification reagents. Role of Cys-300 in restoring thiol sensitivit
Topics: 4-Chloromercuribenzenesulfonate; Amines; Amino Acid Substitution; Biological Transport; Cell Membrane Permeability; Choline; Consensus Sequence; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; GABA Plasma Membrane Transport Proteins; gamma-Aminobutyric Acid; Kinetics; Membrane Proteins; Membrane Transport Modulators; Membrane Transport Proteins; Mesylates; Models, Biological; Organic Anion Transporters; Polyamines; Protein Conformation; Substrate Specificity; Sulfhydryl Compounds; Sulfhydryl Reagents | 1999 |
Paradoxical stimulation of a DEG/ENaC channel by amiloride.
Topics: Acid Sensing Ion Channels; Amiloride; Animals; Binding Sites; Cysteine; Degenerin Sodium Channels; DNA, Complementary; Epithelial Sodium Channels; Humans; Ion Channels; Mesylates; Microinjections; Mutation; Nerve Tissue Proteins; Oocytes; Protons; Sodium Channels; Xenopus laevis; Zinc | 1999 |
Gamma-aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in gamma-aminobutyric acid type A receptors.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acid Substitution; Animals; Cell Membrane; Cysteine; gamma-Aminobutyric Acid; Hydrophobic and Hydrophilic Interactions; Ion Channel Gating; Mesylates; Mutation; Protein Binding; Protein Conformation; Rats; Receptors, GABA-A; Sulfhydryl Compounds; Surface Properties; Water | 1999 |
Time-resolved site-directed spin-labeling studies of bacteriorhodopsin: loop-specific conformational changes in M.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Bacteriorhodopsins; Cysteine; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Kinetics; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Photolysis; Protein Conformation; Protein Structure, Secondary; Purple Membrane; Spectrophotometry, Ultraviolet; Spin Labels | 2000 |
The fourth transmembrane segment of the dopamine D2 receptor: accessibility in the binding-site crevice and position in the transmembrane bundle.
Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cell Line; Cell Membrane; Conserved Sequence; Cysteine; Extracellular Space; Humans; Indicators and Reagents; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Proline; Protein Structure, Secondary; Receptors, Dopamine D2; Recombinant Proteins; Sequence Analysis, Protein; Static Electricity; Templates, Genetic | 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 |
Three pairs of cysteine residues mediate both redox and zn2+ modulation of the nmda receptor.
Topics: Animals; Binding Sites; Cells, Cultured; Cysteine; Dithiothreitol; Dose-Response Relationship, Drug; Drug Synergism; Glycine; Histidine; Mesylates; Mutagenesis, Site-Directed; N-Methylaspartate; Oocytes; Oxidation-Reduction; Patch-Clamp Techniques; Receptors, N-Methyl-D-Aspartate; Structure-Activity Relationship; Sulfhydryl Reagents; Transfection; Xenopus; Zinc | 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 |
Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil.
Topics: Adenosine Triphosphatases; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding Sites; Cysteine; Drug Resistance, Multiple; Humans; Mesylates; Mutagenesis; Verapamil | 2001 |
Chemically charging the pore constriction opens the mechanosensitive channel MscL.
Topics: Biophysical Phenomena; Biophysics; Cysteine; Electrophysiology; Escherichia coli; Escherichia coli Proteins; Ion Channels; Mesylates; Mutagenesis, Site-Directed; Mutagens; Osmosis; Protein Binding; Protein Conformation | 2001 |
The uptake inhibitors cocaine and benztropine differentially alter the conformation of the human dopamine transporter.
Topics: Benztropine; Binding Sites; Binding, Competitive; Carrier Proteins; Cell Membrane; Cocaine; Cysteine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Humans; Indicators and Reagents; Kinetics; Mazindol; Membrane Glycoproteins; Membrane Transport Proteins; Mesylates; Models, Molecular; Nerve Tissue Proteins; Protein Conformation | 2001 |
Cysteine substitutions reveal dual functions of the amino-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating.
Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Alanine; Animals; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Female; Indicators and Reagents; Ion Channel Gating; Mesylates; Xenopus | 2001 |
CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.
Topics: Animals; Anions; Arginine; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Disulfides; Electric Conductivity; Ethyl Methanesulfonate; Female; Humans; Hydrogen-Ion Concentration; Lysine; Membrane Potentials; Mercaptoethanol; Mesylates; Models, Biological; Oocytes; Patch-Clamp Techniques; Perfusion; Xenopus | 2001 |
Cysteine 144 in the third transmembrane domain of the creatine transporter is located close to a substrate-binding site.
Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Biotinylation; Cattle; Cell Line; Chlorine; Creatine; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ions; Kinetics; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rabbits; Rats; Sequence Homology, Amino Acid; Serine; Sodium; Transfection | 2001 |
Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex.
Topics: Aspartic Acid; Bacterial Proteins; Cell Membrane; Cross-Linking Reagents; Cysteine; Dimerization; Disulfides; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Ethylmaleimide; Hydrogen; Immunoblotting; Iodine; Ions; Mesylates; Models, Biological; Mutation; Oxygen; Plasmids; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protons | 2001 |
Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers.
Topics: Calcium-Binding Proteins; Cell Membrane; Cysteine; Electron Spin Resonance Spectroscopy; Glucosidases; Humans; Intracellular Signaling Peptides and Proteins; Lipid Bilayers; Lipids; Membrane Proteins; Mesylates; Models, Biological; Models, Chemical; Myristic Acid; Myristoylated Alanine-Rich C Kinase Substrate; Phosphatidylinositol 4,5-Diphosphate; Phosphoproteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Recombinant Proteins; Spin Labels | 2002 |
Cysteine-scanning mutagenesis study of the sixth transmembrane segment of the Na,K-ATPase alpha subunit.
Topics: Acrylamides; Animals; Bufonidae; Cnidarian Venoms; Cysteine; Indicators and Reagents; Membrane Proteins; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Sodium-Potassium-Exchanging ATPase; Transfection; Xenopus laevis | 2002 |
The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue.
Topics: Animals; Cell Membrane; Cysteine; DNA, Complementary; Histidine; Hydrogen-Ion Concentration; Ions; Kinetics; Membrane Potentials; Mesylates; Mutation; Oocytes; Protein Binding; Protein Structure, Tertiary; Time Factors; Tryptophan; Viral Matrix Proteins; Xenopus laevis | 2002 |
Probing the mechanism of a membrane transport protein with affinity inactivators.
Topics: Affinity Labels; Catalysis; Cysteine; Escherichia coli; Escherichia coli Proteins; Galactosides; Glucosides; Membrane Transport Proteins; Mesylates; Monosaccharide Transport Proteins; Protein Transport; Symporters | 2003 |
Staggering of subunits in NMDAR channels.
Topics: Aminacrine; Amino Acid Sequence; Animals; Cations; Cell Membrane; Cells, Cultured; Cysteine; Extracellular Space; Female; Glutamic Acid; Ion Channel Gating; Ion Channels; Macromolecular Substances; Membrane Potentials; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Protein Conformation; Protein Subunits; Receptors, N-Methyl-D-Aspartate; Sequence Homology, Amino Acid; Silver; Xenopus | 2002 |
Interaction between cysteines introduced into each transmembrane domain of the rat P2X2 receptor.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; Cell Line; Cell Membrane; Cysteine; Dose-Response Relationship, Drug; Humans; Mesylates; Mutagenesis, Site-Directed; Neuropeptides; Protein Binding; Protein Structure, Tertiary; Rats; Receptors, Purinergic P2; Receptors, Purinergic P2X2 | 2003 |
Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding Sites; Cell Line; Cysteine; Humans; Kidney; Mesylates; Mutagenesis; Protein Structure, Tertiary; Verapamil | 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 |
Methanethiosulfonate-modification alters local anesthetic block in rNav1.4 cysteine-substituted mutants S1276C and L1280C.
Topics: Anesthetics, Local; Animals; Bupivacaine; Cysteine; Humans; Ion Channel Gating; Kidney; Membrane Potentials; Mesylates; Muscle Proteins; Muscle, Skeletal; Mutation; NAV1.4 Voltage-Gated Sodium Channel; Rats; Sodium Channels; Structure-Activity Relationship | 2003 |
Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents.
Topics: Amino Acid Substitution; Animals; Cell Membrane Permeability; Chloride Channels; Cysteine; Indicators and Reagents; Ion Channel Gating; Mesylates; Point Mutation; Protein Conformation; Structure-Activity Relationship; Thiosulfonic Acids; Torpedo | 2003 |
Accessibility of cysteine residues in a cytoplasmic loop of CitS of Klebsiella pneumoniae is controlled by the catalytic state of the transporter.
Topics: Bacterial Proteins; Binding Sites; Carbon Isotopes; Carrier Proteins; Catalysis; Cell Membrane; Cell Membrane Permeability; Citric Acid; Cysteine; Cytoplasm; Ethylmaleimide; Klebsiella pneumoniae; Maleimides; Mesylates; Proton-Motive Force; Sodium; Transport Vesicles | 2003 |
Different gating mechanisms in glutamate receptor and K+ channels.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cell Line; Cells, Cultured; Cysteine; Electric Conductivity; Glycine; Humans; Indicators and Reagents; Ion Channel Gating; Mesylates; Models, Molecular; Molecular Sequence Data; Potassium Channels; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Subunits; Receptors, AMPA; Receptors, Glutamate; Sequence Alignment; Xenopus | 2003 |
Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites.
Topics: Adenosine Triphosphatases; ATP Binding Cassette Transporter, Subfamily B, Member 1; Benzimidazoles; Binding Sites; Biological Transport; Calcium Channel Blockers; Cell Line; Colchicine; Cysteine; Disulfides; DNA, Complementary; Dose-Response Relationship, Drug; Fluoresceins; Fluorescent Dyes; Histidine; Humans; Mesylates; Models, Biological; Models, Chemical; Mutation; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodamines; Verapamil | 2003 |
Site-directed sulfhydryl labeling of the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae: helix VIII comprises a portion of the sodium ion channel.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Carboxy-Lyases; Cysteine; Indicators and Reagents; Klebsiella pneumoniae; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protein Subunits; Protein Transport; Sodium Channels; Sodium-Potassium-Exchanging ATPase; Structure-Activity Relationship; Sulfhydryl Compounds | 2003 |
A microdomain formed by the extracellular ends of the transmembrane domains promotes activation of the G protein-coupled alpha-factor receptor.
Topics: Amino Acid Sequence; Binding Sites; Biotin; Cell Division; Cysteine; Genes, Reporter; Ligands; Mesylates; Models, Molecular; Mutation; Phenotype; Pheromones; Protein Binding; Protein Structure, Secondary; Receptors, G-Protein-Coupled; Receptors, Mating Factor; Receptors, Peptide; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Signal Transduction; Transcription Factors | 2004 |
Transmembrane domain 5 of the LdNT1.1 nucleoside transporter is an amphipathic helix that forms part of the nucleoside translocation pathway.
Topics: Adenosine; Amino Acid Substitution; Animals; Biological Transport; Cells, Cultured; Cysteine; Mesylates; Mutagenesis, Site-Directed; Nucleoside Transport Proteins; Nucleosides; Oocytes; Protein Conformation; Protein Structure, Tertiary; Protozoan Proteins; Sulfhydryl Compounds; Uridine; Xenopus | 2004 |
Channel gating of the glycine receptor changes accessibility to residues implicated in receptor potentiation by alcohols and anesthetics.
Topics: Alcohols; Anesthetics; Animals; Binding Sites; Cell Membrane; Cysteine; Electrophysiology; Female; Gene Expression; Humans; Ion Channel Gating; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Secondary; Receptors, Glycine; Structure-Activity Relationship; Transfection; 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 |
The mitochondrial tricarboxylate carrier of silver eel: chemical modification by sulfhydryl reagents.
Topics: Anguilla; Animals; Carrier Proteins; Cysteine; Maleimides; Mercury Compounds; Mesylates; Mitochondria, Liver; Proteolipids; Sulfhydryl Reagents | 2004 |
Structure-function relations of the first and fourth predicted extracellular linkers of the type IIa Na+/Pi cotransporter: I. Cysteine scanning mutagenesis.
Topics: Amino Acid Sequence; Animals; Cell Membrane; Cells, Cultured; Cysteine; Dose-Response Relationship, Drug; Extracellular Fluid; Membrane Potentials; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Phosphates; Protein Subunits; Recombinant Proteins; Sodium-Phosphate Cotransporter Proteins; Structure-Activity Relationship; Symporters; Xenopus laevis | 2004 |
Structure-function relations of the first and fourth extracellular linkers of the type IIa Na+/Pi cotransporter: II. Substrate interaction and voltage dependency of two functionally important sites.
Topics: Amino Acid Sequence; Animals; Cell Membrane; Cells, Cultured; Cysteine; Dose-Response Relationship, Drug; Extracellular Fluid; Membrane Potentials; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Phosphates; Protein Subunits; Recombinant Proteins; Sodium-Phosphate Cotransporter Proteins; Structure-Activity Relationship; Symporters; Xenopus laevis | 2004 |
Intracellular thiol-mediated modulation of epithelial sodium channel activity.
Topics: Animals; Cadmium; Calcium; Cell Membrane; Chelating Agents; Copper; Cysteine; Dithiothreitol; Edetic Acid; Egtazic Acid; Electrophysiology; Epithelial Sodium Channels; Female; Hydrogen-Ion Concentration; Ions; Mesylates; Models, Biological; Mutagenesis, Site-Directed; Oocytes; Oxygen; Protein Conformation; Protein Structure, Tertiary; RNA, Complementary; Sodium; Sodium Channels; Sulfhydryl Compounds; Time Factors; Xenopus laevis; Zinc | 2005 |
Carboxy-terminal truncations modify the outer pore vestibule of muscle chloride channels.
Topics: Animals; Anions; Cell Line; Chloride Channels; Cysteine; Cystine; DNA, Complementary; Electrophysiology; Humans; Indicators and Reagents; Ion Channel Gating; Ions; Kinetics; Macromolecular Substances; Mesylates; Models, Chemical; Muscles; Mutation; Plasmids; Protein Conformation; Protein Isoforms; Protein Structure, Tertiary; Time Factors | 2005 |
Exploring the binding domain of EmrE, the smallest multidrug transporter.
Topics: Antiporters; Binding Sites; Cell Membrane; Cysteine; Dimerization; Dose-Response Relationship, Drug; Drug Resistance, Multiple, Bacterial; Escherichia coli; Escherichia coli Proteins; Fluoresceins; Fluorescent Dyes; Glutamic Acid; Hydrogen-Ion Concentration; Indicators and Reagents; Membrane Proteins; Membrane Transport Proteins; Mesylates; Mutagenesis, Site-Directed; Onium Compounds; Organophosphorus Compounds; Plasmids; Protein Binding; Protein Structure, Tertiary; Protons; Substrate Specificity | 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 |
Cysteine-scanning mutagenesis and thiol modification of the Rickettsia prowazekii ATP/ADP translocase: characterization of TMs IV-VII and IX-XII and their accessibility to the aqueous translocation pathway.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Biological Transport; Cell Membrane; Cysteine; Mesylates; Mitochondrial ADP, ATP Translocases; Molecular Sequence Data; Mutagenesis; Protein Conformation; Rickettsia prowazekii; Sulfhydryl Compounds | 2006 |
Voltage clamp fluorometric measurements on a type II Na+-coupled Pi cotransporter: shedding light on substrate binding order.
Topics: Animals; Biological Transport; Cysteine; Electrophysiology; Female; Flounder; Fluorometry; Lithium; Mesylates; Models, Biological; Oocytes; Patch-Clamp Techniques; Phosphates; Protein Binding; Protein Conformation; Sodium; Sodium-Phosphate Cotransporter Proteins, Type II; Substrate Specificity; Xenopus laevis | 2006 |
Conformational dynamics of loop 262-274 in G- and F-actin.
Topics: Actin Cytoskeleton; Actins; Bridged Bicyclo Compounds; Cross-Linking Reagents; Cysteine; Disulfides; Electron Spin Resonance Spectroscopy; Hydrophobic and Hydrophilic Interactions; Mesylates; Myosin Subfragments; Phalloidine; Protein Conformation; Saccharomyces cerevisiae; Tropomyosin | 2006 |
Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket.
Topics: Adenosine Triphosphatases; Amino Acid Sequence; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding Sites; Cell Membrane; Cells, Cultured; Cross-Linking Reagents; Cysteine; Disulfides; Enzyme Activation; Humans; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Structure, Secondary; Substrate Specificity; Vanadates; Verapamil | 2006 |
Localization of the pH gate in Kir1.1 channels.
Topics: Animals; Cysteine; Cytoplasm; Female; Hydrogen-Ion Concentration; In Vitro Techniques; Indicators and Reagents; Ion Channel Gating; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Potassium; Potassium Channels, Inwardly Rectifying; Xenopus laevis | 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 |
A cysteine-scanning mutagenesis study of transmembrane domain 8 of the electrogenic sodium/bicarbonate cotransporter NBCe1.
Topics: 4-Chloromercuribenzenesulfonate; Animals; Biological Transport; Cysteine; Female; Gene Expression Regulation; Mesylates; Microelectrodes; Mutagenesis; Oocytes; Patch-Clamp Techniques; Protein Structure, Tertiary; Rats; RNA, Complementary; Sodium-Bicarbonate Symporters; Sulfhydryl Reagents; Xenopus laevis | 2006 |
Dynamic modification of a mutant cytoplasmic cysteine residue modulates the conductance of the human 5-HT3A receptor.
Topics: Amino Acid Substitution; Arginine; Biological Transport; Cysteine; Cytoplasm; Electrophysiology; Humans; Mesylates; Mutation; Receptors, Serotonin, 5-HT3; Static Electricity | 2007 |
Functional role of extracellular loop cysteine residues of the epithelial Na+ channel in Na+ self-inhibition.
Topics: Amino Acid Substitution; Animals; Cysteine; Disulfides; Epithelial Sodium Channels; Female; Gene Expression; Indicators and Reagents; Ion Transport; Membrane Potentials; Mesylates; Mice; Mutation, Missense; Oocytes; Patch-Clamp Techniques; Protein Structure, Quaternary; Protein Structure, Tertiary; Sodium; Xenopus laevis | 2007 |
KCNE1 and KCNE3 stabilize and/or slow voltage sensing S4 segment of KCNQ1 channel.
Topics: Animals; Binding Sites; Cysteine; Disulfides; Female; Humans; Ion Channel Gating; KCNQ1 Potassium Channel; Kinetics; Membrane Potentials; Mesylates; Mice; Models, Biological; Mutagenesis, Site-Directed; Oocytes; Potassium Channels, Voltage-Gated; Protein Binding; Protein Structure, Tertiary; Rats; Sulfhydryl Reagents; Xenopus | 2007 |
A proton-mediated conformational shift identifies a mobile pore-lining cysteine residue (Cys-561) in human concentrative nucleoside transporter 3.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acid Sequence; Animals; Cysteine; Electrophysiology; Humans; Membrane Transport Proteins; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Oocytes; Patch-Clamp Techniques; Protein Structure, Tertiary; Protons; Sequence Alignment; Uridine; Xenopus laevis | 2008 |
Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Binding Sites; Carbon Radioisotopes; Cell Membrane; Cysteine; Escherichia coli; Ethylmaleimide; Mesylates; Mitochondrial Proton-Translocating ATPases; Models, Molecular; Mutant Proteins; Protein Subunits; Proton Pumps; Silver; Staining and Labeling; Sulfhydryl Reagents | 2008 |
Structural mechanisms underlying benzodiazepine modulation of the GABA(A) receptor.
Topics: Allosteric Regulation; Animals; Benzodiazepines; Binding Sites; Carbolines; Convulsants; Cysteine; Dose-Response Relationship, Drug; gamma-Aminobutyric Acid; Indicators and Reagents; Ion Channel Gating; Larva; Membrane Potentials; Mesylates; Microinjections; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Binding; Rats; Receptors, GABA-A; Structure-Activity Relationship; Xenopus | 2008 |
Cysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Conserved Sequence; Cysteine; Electrophysiology; Female; Humans; Mesylates; Molecular Sequence Data; Mutation; Oocytes; Patch-Clamp Techniques; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Receptors, Purinergic P2X4; Sequence Alignment; Xenopus laevis | 2008 |
Use of mass spectrometry to probe the nucleophilicity of cysteinyl residues of prolyl hydroxylase domain 2.
Topics: Alkylating Agents; Amino Acid Substitution; Catalytic Domain; Cysteine; Escherichia coli; Ethylmaleimide; Gene Expression; Humans; Hypoxia-Inducible Factor-Proline Dioxygenases; Mesylates; Procollagen-Proline Dioxygenase; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spin Labels; Sulfhydryl Compounds; Sulfhydryl Reagents | 2009 |
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 |
Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition.
Topics: Amino Acid Substitution; Binding Sites; Biological Transport; Crystallization; Cysteine; Escherichia coli; Escherichia coli Proteins; Galactose; Lactose; Membrane Transport Proteins; Mesylates; Models, Molecular; Monosaccharide Transport Proteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Substrate Specificity; Symporters; X-Ray Diffraction | 2011 |
Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.
Topics: Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Cytoplasm; Humans; Membrane Proteins; Mesylates; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Protein Structure, Secondary; Sequence Alignment | 2011 |
Identification of cysteines involved in the effects of methanethiosulfonate reagents on human equilibrative nucleoside transporter 1.
Topics: Amino Acid Sequence; Animals; Cell Line; Cysteine; Equilibrative Nucleoside Transporter 1; Humans; Indicators and Reagents; Mesylates; Molecular Sequence Data; Mutation; Swine | 2011 |
Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant.
Topics: Amino Acid Sequence; Animals; Cricetinae; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Mesylates; Patch-Clamp Techniques | 2011 |
Role of the juxtamembrane region of cytoplasmic loop 3 in the gating and conductance of the cystic fibrosis transmembrane conductance regulator chloride channel.
Topics: Adenosine Triphosphate; Animals; Cell Line; Chloride Channels; Cricetinae; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Cytoplasm; Humans; Ion Transport; Mesylates; Mutation; Patch-Clamp Techniques; Protein Conformation; Protein Structure, Tertiary | 2012 |
Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeation.
Topics: Animals; Cell Membrane; Chlorides; CHO Cells; Cricetinae; Cricetulus; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Ion Channel Gating; Mesylates; Mutation, Missense; Permeability; Protein Structure, Tertiary | 2013 |
Large scale production of the active human ASCT2 (SLC1A5) transporter in Pichia pastoris--functional and kinetic asymmetry revealed in proteoliposomes.
Topics: Amino Acid Transport System ASC; Biological Transport; Cloning, Molecular; Cysteine; Gene Expression; Glutamine; Humans; Hydrogen-Ion Concentration; Kinetics; Mercury Compounds; Mesylates; Minor Histocompatibility Antigens; Models, Molecular; Pichia; Proteolipids; Sequence Homology, Amino Acid; Substrate Specificity | 2013 |
GABA(A) receptor transmembrane amino acids are critical for alcohol action: disulfide cross-linking and alkyl methanethiosulfonate labeling reveal relative location of binding sites.
Topics: Amino Acids; Animals; Binding Sites; Central Nervous System Depressants; Cloning, Molecular; Cross-Linking Reagents; Cysteine; Disulfides; Dose-Response Relationship, Drug; Electrophysiological Phenomena; Ethanol; GABA Agents; gamma-Aminobutyric Acid; Humans; Mesylates; Models, Molecular; Oocytes; Oxidation-Reduction; Receptors, GABA-A; Xenopus laevis | 2014 |
Determinants of Cation Permeation and Drug Sensitivity in Predicted Transmembrane Helix 9 and Adjoining Exofacial Re-entrant Loop 5 of Na+/H+ Exchanger NHE1.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cations; Cysteine; Drug Resistance; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Rats; Sequence Alignment; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers; Substrate Specificity | 2015 |
Cysteine-Specific Labeling of Proteins with a Nitroxide Biradical for Dynamic Nuclear Polarization NMR.
Topics: Anabaena; Cyclic N-Oxides; Cysteine; Glycerol; Mesylates; Molecular Structure; Mutation; Nitrogen Isotopes; Nitrogen Oxides; Nuclear Magnetic Resonance, Biomolecular; Propanols; Protons; Sensory Rhodopsins; Solvents; Temperature; Water | 2015 |
A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.
Topics: Anisotropy; Calcium-Binding Proteins; Crystallography, X-Ray; Cysteine; Electron Spin Resonance Spectroscopy; Humans; Lipid Bilayers; Membrane Proteins; Mesylates; Models, Molecular; Stereoisomerism | 2016 |
Pinning Down the Mechanism of Transport: Probing the Structure and Function of Transporters Using Cysteine Cross-Linking and Site-Specific Labeling.
Topics: Biochemistry; Biological Transport; Carrier Proteins; Cross-Linking Reagents; Cysteine; Electrophoresis, Polyacrylamide Gel; Maleimides; Mass Spectrometry; Mercury; Mesylates; Protein Conformation | 2017 |
Rapid Mapping of Protein Interactions Using Tag-Transfer Photocrosslinkers.
Topics: Cross-Linking Reagents; Cysteine; Mass Spectrometry; Mesylates; Molecular Structure; Photochemical Processes; Protein Interaction Maps; Proteins | 2018 |
In situ observation of conformational dynamics and protein ligand-substrate interactions in outer-membrane proteins with DEER/PELDOR spectroscopy.
Topics: Bacterial Outer Membrane Proteins; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Mesylates; Protein Conformation; Spin Labels | 2019 |