cysteine and methanethiosulfonate

cysteine has been researched along with methanethiosulfonate in 89 studies

Research

Studies (89)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's21 (23.60)18.2507
2000's52 (58.43)29.6817
2010's16 (17.98)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Akabas, MH; Archdeacon, P; Karlin, A; Kaufmann, C1
Chen, J; Fu, D; Javitch, JA; Karlin, A1
Brown, AM; Kirsch, GE; Pascual, JM; Shieh, CC1
Karlin, A; Stauffer, DA1
Akabas, MH; Cheung, M2
Chen, J; Fu, D; Javitch, JA1
Howells, RD; Shahrestanifar, MS1
Fetrow, JS; Qu, K; Scholes, CP; Sienkiewicz, A; Vaughn, JL1
Cao, Z; Feix, JB; Foster, SB; Jiang, X; Klebba, PE; Newton, SM; Payne, MA1
Buell, G; Newbolt, A; North, RA; Rassendren, F; Surprenant, A1
Feix, JB; Klug, CS; Su, W1
Grunewald, M; Kanner, BI; Kavanaugh, MP; Zarbiv, R1
Ferrer, JV; Javitch, JA1
Jones, LR; Karim, CB; Karim, J; Stamm, JD; Thomas, DD1
Karlin, A; Pascual, JM1
Jones, JB; Khumtaveeporn, K; Plettner, E; Shang, X1
Kriegler, S; Sudweeks, S; Yakel, JL1
Hu, LA; King, SC1
Adams, CM; Snyder, PM; Welsh, MJ1
Akabas, MH; Williams, DB1
Hubbell, WL; Khorana, HG; Mollaaghababa, R; Steinhoff, HJ1
Ballesteros, JA; Chen, J; Chiappa, V; Javitch, JA; Shi, L; Simpson, MM; Visiers, I; Weinstein, H1
Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Xu, W1
Chen, HV; Choi, Y; Lipton, SA1
Loussouarn, G; Masia, R; Nichols, CG; Phillips, LR; Rose, T1
Clarke, DM; Loo, TW1
Batiza, A; Kung, C; Yoshimura, K1
Berfield, JL; Ferrer, JV; Javitch, JA; Reith, ME; Wang, LC1
Fu, J; Kirk, KL1
Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR1
Christie, DL; Dodd, JR2
Blair, DF; Braun, TF1
Cafiso, DS; Ferguson, CG; Prestwich, GD; Rauch, ME1
Guennoun, S; Horisberger, JD1
Lamb, RA; Pinto, LH; Tang, Y; Zaitseva, F1
Guan, L; Hideg, K; Kaback, HR; Kálai, T; Sahin-Tóth, M1
Rooney, L; Sobolevsky, AI; Wollmuth, LP1
Bailey, RJ; Jiang, LH; North, RA; Spelta, V; Surprenant, A1
Bartlett, MC; Clarke, DM; Loo, TW3
Beaulieu, ME; Boucard, AA; Escher, E; Guillemette, G; Lavigne, P; Leduc, R; Roy, M1
O'Reilly, JP; Wang, GK; Wang, SY1
Chen, TY; Lin, CW1
Lolkema, JS; Sobczak, I1
Sobolevsky, AI; Wollmuth, LP; Yelshansky, MV1
Dimroth, P; Pos, KM; Wild, MR1
Duell, K; Konopka, JB; Lin, JC1
Conklin, D; Landfear, SM; Valdés, R; Vasudevan, G1
Harris, RA; Lobo, IA; Mascia, MP; Trudell, JR1
Alexeyev, MF; Audia, JP; Daugherty, RM; Roberts, RA; Winkler, HH1
Capobianco, L; Ferramosca, A; Impagnatiello, T; Zara, V1
Bacconi, A; Biber, J; Ehnes, C; Forster, IC; Kohler, K; Murer, H; Stange, G1
Bacconi, A; Biber, J; Ehnes, C; Forster, IC; Kohler, K; Murer, H1
Gautschi, I; Kellenberger, S; Pfister, Y; Schild, L1
Fahlke, C; Hebeisen, S1
Schuldiner, S; Sharoni, M; Steiner-Mordoch, S1
Audia, JP; Roberts, RA; Winkler, HH1
Forster, IC; Murer, H; Virkki, LV1
Altenbach, C; Hideg, K; Hubbell, WL; Phillips, M; Reisler, E; Rubenstein, PA; Shvetsov, A; Stamm, JD; Warshaviak, D1
Palmer, LG; Sackin, H; Zhang, YY1
Banerjee, A; Hussainzada, N; Swaan, PW1
Bevensee, MO; McAlear, SD1
Carland, JE; Cooper, MA; Deeb, TZ; Hales, TG; Lambert, JJ; Livesey, MR; Peters, JA1
Bruns, JB; Hughey, RP; Kleyman, TR; Maarouf, AB; Sheng, S1
Kubo, Y; Nakajo, K1
Baldwin, SA; Cass, CE; Karpinski, E; Lin, CC; Ng, AM; Slugoski, MD; Smith, KM; Yao, SY; Young, JD; Zhang, J1
Fillingame, RH; Steed, PR1
Czajkowski, C; Hanson, SM1
Digby, HR; El Ajouz, S; Evans, RJ; Kara, M; Roberts, JA; Sutcliffe, MJ1
Chowdhury, R; Flashman, E; Mecinović, J; Schofield, CJ1
Chen, TY; Yu, WP; Zhang, XD1
Nishiya, T; Uehara, T1
Abramson, J; Chaptal, V; Guan, L; Kaback, HR; Kwon, S; Sawaya, MR1
El Hiani, Y; Linsdell, P; Wang, W1
Cunningham, FK; Hammond, JR; Hughes, SJ; Park, JS1
El Hiani, Y; Linsdell, P; Qian, F1
El Hiani, Y; Linsdell, P1
Bai, Y; Gao, X; Hwang, TC1
Galluccio, M; Hedfalk, K; Indiveri, C; Pingitore, P; Pochini, L; Scalise, M1
Borghese, CM; Harris, RA; Hicks, JA; Lapid, DJ; Trudell, JR1
Boucher, A; Jinadasa, T; Josephson, CB; Orlowski, J1
Brown, LS; Caporini, MA; Good, DB; Ladizhansky, V; Ljumovic, M; Marek, A; Milikisiyants, S; Munro, RA; Rosay, M; Smirnov, AI; Voinov, MA; Ward, ME1
Binder, BP; James, ZM; McCaffrey, JE; Svensson, B; Thomas, DD1
Mindell, JA; Mulligan, C1
Brockwell, DJ; Calabrese, AN; Horne, JE; Kapur, N; Levenstein, MA; Radford, SE; Walko, M; Wilson, AJ1
Barth, K; Cafiso, DS; Jaumann, EA; Joseph, B; Prisner, TF; Sikora, A1

Reviews

1 review(s) available for cysteine and methanethiosulfonate

ArticleYear
Screening systems for the identification of S-nitrosylated proteins.
    Nitric oxide : biology and chemistry, 2011, Aug-01, Volume: 25, Issue:2

    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

Other Studies

88 other study(ies) available for cysteine and methanethiosulfonate

ArticleYear
Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit.
    Neuron, 1994, Volume: 13, Issue:4

    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.
    Neuron, 1995, Volume: 14, Issue:4

    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.
    Neuron, 1995, Volume: 14, Issue:5

    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.
    Biochemistry, 1994, Jun-07, Volume: 33, Issue:22

    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.
    Biophysical journal, 1996, Volume: 70, Issue:6

    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.
    Biochemistry, 1995, Dec-19, Volume: 34, Issue:50

    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.
    Neurochemical research, 1996, Volume: 21, Issue:11

    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.
    Biochemistry, 1997, Mar-11, Volume: 36, Issue:10

    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.
    The Journal of general physiology, 1997, Volume: 109, Issue:3

    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.
    Science (New York, N.Y.), 1997, May-23, Volume: 276, Issue:5316

    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.
    The EMBO journal, 1997, Jun-16, Volume: 16, Issue:12

    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.
    Biochemistry, 1997, Oct-21, Volume: 36, Issue:42

    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.
    The Journal of biological chemistry, 1998, Jun-05, Volume: 273, Issue:23

    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.
    Proceedings of the National Academy of Sciences of the United States of America, 1998, Aug-04, Volume: 95, Issue:16

    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.
    Biochemistry, 1998, Sep-01, Volume: 37, Issue:35

    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.
    The Journal of general physiology, 1998, Volume: 112, Issue:5

    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.
    Bioorganic & medicinal chemistry letters, 1998, Sep-08, Volume: 8, Issue:17

    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.
    The Journal of biological chemistry, 1999, Feb-12, Volume: 274, Issue:7

    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
    The Biochemical journal, 1999, May-01, Volume: 339 ( Pt 3)

    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.
    The Journal of biological chemistry, 1999, May-28, Volume: 274, Issue:22

    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.
    Biophysical journal, 1999, Volume: 77, Issue:5

    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.
    Biochemistry, 2000, Feb-08, Volume: 39, Issue:5

    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.
    Biochemistry, 2000, Oct-10, Volume: 39, Issue:40

    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.
    Biochemistry, 2000, Nov-14, Volume: 39, Issue:45

    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.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001, Jan-15, Volume: 21, Issue:2

    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.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Mar-27, Volume: 98, Issue:7

    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.
    The Journal of biological chemistry, 2001, May-04, Volume: 276, Issue:18

    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.
    Biophysical journal, 2001, Volume: 80, Issue:5

    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.
    The Journal of biological chemistry, 2001, Aug-03, Volume: 276, Issue:31

    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.
    The Journal of biological chemistry, 2001, Sep-21, Volume: 276, Issue:38

    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.
    The Journal of general physiology, 2001, Volume: 118, Issue:4

    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.
    The Journal of biological chemistry, 2001, Dec-14, Volume: 276, Issue:50

    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.
    Biochemistry, 2001, Oct-30, Volume: 40, Issue:43

    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.
    The Journal of biological chemistry, 2002, Apr-19, Volume: 277, Issue:16

    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.
    FEBS letters, 2002, Feb-27, Volume: 513, Issue:2-3

    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.
    The Journal of biological chemistry, 2002, Oct-18, Volume: 277, Issue:42

    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.
    The Journal of biological chemistry, 2003, Mar-21, Volume: 278, Issue:12

    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.
    Biophysical journal, 2002, Volume: 83, Issue:6

    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.
    British journal of pharmacology, 2003, Volume: 138, Issue:1

    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.
    The Journal of biological chemistry, 2003, Jun-06, Volume: 278, Issue:23

    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.
    The Journal of biological chemistry, 2003, Sep-19, Volume: 278, Issue:38

    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.
    The Journal of membrane biology, 2003, May-01, Volume: 193, Issue:1

    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.
    The Journal of general physiology, 2003, Volume: 122, Issue:2

    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.
    Biochemistry, 2003, Aug-19, Volume: 42, Issue:32

    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.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2003, Aug-20, Volume: 23, Issue:20

    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.
    The Journal of biological chemistry, 2003, Dec-12, Volume: 278, Issue:50

    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.
    Biochemistry, 2003, Oct-14, Volume: 42, Issue:40

    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.
    Molecular and cellular biology, 2004, Volume: 24, Issue:5

    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.
    Biochemistry, 2004, Jun-01, Volume: 43, Issue:21

    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.
    The Journal of biological chemistry, 2004, Aug-06, Volume: 279, Issue:32

    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.
    Biochemistry, 2004, Jun-08, Volume: 43, Issue:22

    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.
    Journal of biochemistry and molecular biology, 2004, Sep-30, Volume: 37, Issue:5

    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.
    The Journal of general physiology, 2004, Volume: 124, Issue:5

    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.
    The Journal of general physiology, 2004, Volume: 124, Issue:5

    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.
    The Journal of biological chemistry, 2005, Mar-04, Volume: 280, Issue:9

    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.
    Biophysical journal, 2005, Volume: 89, Issue:3

    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.
    The Journal of biological chemistry, 2005, Sep-23, Volume: 280, Issue:38

    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.
    The Journal of biological chemistry, 2005, Sep-23, Volume: 280, Issue:38

    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.
    Biochemistry, 2006, Feb-28, Volume: 45, Issue:8

    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.
    The Journal of general physiology, 2006, Volume: 127, Issue:5

    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.
    Biochemistry, 2006, May-23, Volume: 45, Issue:20

    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.
    The Biochemical journal, 2006, Oct-15, Volume: 399, Issue:2

    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.
    Biophysical journal, 2006, Oct-15, Volume: 91, Issue:8

    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.
    Molecular pharmacology, 2006, Volume: 70, Issue:5

    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.
    The Journal of biological chemistry, 2006, Oct-27, Volume: 281, Issue:43

    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.
    The Journal of biological chemistry, 2007, Mar-02, Volume: 282, Issue:9

    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.
    The Journal of biological chemistry, 2007, Jul-13, Volume: 282, Issue:28

    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.
    The Journal of general physiology, 2007, Volume: 130, Issue:3

    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.
    The Journal of biological chemistry, 2008, Mar-28, Volume: 283, Issue:13

    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.
    The Journal of biological chemistry, 2008, May-02, Volume: 283, Issue:18

    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.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008, Mar-26, Volume: 28, Issue:13

    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.
    The Journal of biological chemistry, 2008, Jul-18, Volume: 283, Issue:29

    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.
    Analytical biochemistry, 2009, Oct-15, Volume: 393, Issue: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.
    Biophysical journal, 2010, Feb-03, Volume: 98, Issue:3

    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.
    Proceedings of the National Academy of Sciences of the United States of America, 2011, Jun-07, Volume: 108, Issue:23

    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.
    The Journal of general physiology, 2011, Volume: 138, Issue:2

    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.
    Molecular pharmacology, 2011, Volume: 80, Issue:4

    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.
    Pflugers Archiv : European journal of physiology, 2011, Volume: 462, Issue:4

    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.
    Biochemistry, 2012, May-15, Volume: 51, Issue:19

    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.
    Biophysical journal, 2013, Feb-19, Volume: 104, Issue:4

    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.
    Biochimica et biophysica acta, 2013, Volume: 1828, Issue:9

    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.
    Journal of neurochemistry, 2014, Volume: 128, Issue:3

    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.
    The Journal of biological chemistry, 2015, Jul-17, Volume: 290, Issue:29

    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.
    The journal of physical chemistry. B, 2015, Aug-13, Volume: 119, Issue:32

    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.
    Journal of magnetic resonance (San Diego, Calif. : 1997), 2016, Volume: 262

    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.
    Methods in enzymology, 2017, Volume: 594

    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.
    Angewandte Chemie (International ed. in English), 2018, 12-17, Volume: 57, Issue:51

    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.
    Nature protocols, 2019, Volume: 14, Issue:8

    Topics: Bacterial Outer Membrane Proteins; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Mesylates; Protein Conformation; Spin Labels

2019