cysteine and 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid

cysteine has been researched along with 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid in 25 studies

Research

Studies (25)

Timeframe	Studies, this research(%)	All Research%
pre-1990	3 (12.00)	18.7374
1990's	13 (52.00)	18.2507
2000's	8 (32.00)	29.6817
2010's	1 (4.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hiratsuka, T	2
Cerione, RA; Phillips, WJ	1
Johnson, JD; Mills, JS; Nemcek, K; Walsh, MP	1
Bose, SK; Chakrabarti, B; Mandal, K; Siezen, RJ	1
Gennis, RB; Koland, JG	1
Cerione, RA; Erickson, JW; Mittal, R	1
Frillingos, S; Kaback, HR; Wu, J	1
Frillingos, S; Kaback, HR; Voss, J; Wu, J	1
Kaback, HR; Wu, J	1
Liu, R; Sharom, FJ	1
Buckley, JT; Feil, SC; Nelson, KL; Parker, MW; Raja, SM; Rossjohn, J; van der Goot, FG	1
Homma, K; Maruta, S; Ohki, T	1
Boorsma, A; de Wit, JG; Driessen, AJ; Fekkes, P; Friesen, RH	1
Meuller, J; Rydström, J	1
Gatto, C; Holden, JP; Kaplan, JH; Thornewell, SJ	1
Eisses, JF; Hu, YK; Kaplan, JH	1
Altenbach, C; Hideg, K; Hubbell, WL; Kaback, HR; Kálai, T; Zhao, M	1
Althage, M; Bizouarn, T; Rydström, J	1
Epps, DE; Vosters, AF	1
Kaback, HR; Smirnova, IN	1
Ding, H; Mukerji, I; Oliver, D	1
Huang, Y; Huang, Z	1
Ermolova, NV; Kaback, HR; Kasho, VN; Smirnova, IN	1
Kaback, HR; Kasho, V; Smirnova, I; Sugihara, J	1

Other Studies

25 other study(ies) available for cysteine and 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid

Article	Year
Movement of Cys-697 in myosin ATPase associated with ATP hydrolysis. The Journal of biological chemistry, 1992, Jul-25, Volume: 267, Issue:21 Topics: Adenosine Diphosphate; Adenosine Triphosphate; Anilino Naphthalenesulfonates; Animals; Cysteine; Hydrolysis; Hydroxylamine; Hydroxylamines; Myosins; Rabbits; Spectrometry, Fluorescence; Sulfhydryl Reagents	1992
Spatial proximity of ATP-sensitive tryptophanyl residue(s) and Cys-697 in myosin ATPase. The Journal of biological chemistry, 1992, Jul-25, Volume: 267, Issue:21 Topics: Adenosine Diphosphate; Adenosine Triphosphate; Anilino Naphthalenesulfonates; Animals; Cysteine; Myosins; Rabbits; Spectrometry, Fluorescence; Sulfhydryl Reagents; Tryptophan	1992
Labeling of the beta gamma subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions. The Journal of biological chemistry, 1991, Jun-15, Volume: 266, Issue:17 Topics: Aluminum; Aluminum Compounds; Anilino Naphthalenesulfonates; Animals; Cattle; Cysteine; Fluorides; Fluorine; GTP Phosphohydrolases; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Diphosphate; Kinetics; Macromolecular Substances; Rhodopsin; Rod Cell Outer Segment; Spectrometry, Fluorescence; Sulfhydryl Reagents; Transducin	1991
Biologically active fluorescent derivatives of spinach calmodulin that report calmodulin target protein binding. Biochemistry, 1988, Feb-09, Volume: 27, Issue:3 Topics: Anilino Naphthalenesulfonates; Animals; Brain; Calcium; Calmodulin; Calmodulin-Binding Proteins; Cattle; Cysteine; Kinetics; Myosin-Light-Chain Kinase; Plants; Spectrometry, Fluorescence; Sulfhydryl Reagents	1988
Structure and stability of gamma-crystallins. II. Differences in microenvironments and spatial arrangements of cysteine residues. Biochimica et biophysica acta, 1987, Feb-25, Volume: 911, Issue:3 Topics: Anilino Naphthalenesulfonates; Animals; Cattle; Chemical Phenomena; Chemistry, Physical; Crystallins; Cysteine; Mathematics	1987
Proximity of reactive cysteine residue and flavin in Escherichia coli pyruvate oxidase as estimated by fluorescence energy transfer. Biochemistry, 1982, Aug-31, Volume: 21, Issue:18 Topics: Anilino Naphthalenesulfonates; Chemical Phenomena; Chemistry, Physical; Cysteine; Escherichia coli; Fluorescence Polarization; Fluorescent Dyes; Naphthalenesulfonates; Pyruvate Oxidase; Spectrometry, Fluorescence; Thiamine Pyrophosphate	1982
Use of resonance energy transfer to determine the proximity of the guanine nucleotide binding site of transducin relative to a conformationally-sensitive site on the gamma subunit of the cyclic GMP phosphodiesterase. Biochemistry, 1995, Jul-11, Volume: 34, Issue:27 Topics: 3',5'-Cyclic-GMP Phosphodiesterases; Amino Acid Sequence; Anilino Naphthalenesulfonates; Animals; Binding Sites; Cattle; Cysteine; Energy Transfer; Eosine Yellowish-(YS); Fluorescent Dyes; Guanine Nucleotides; Lysine; Molecular Sequence Data; Sulfhydryl Reagents; Transducin	1995
Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopy. Biochemistry, 1995, Jul-04, Volume: 34, Issue:26 Topics: Amino Acid Sequence; Anilino Naphthalenesulfonates; Carbohydrate Sequence; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Fluorescent Dyes; Kinetics; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Pyrenes; Recombinant Proteins; Spectrometry, Fluorescence; Sulfhydryl Reagents; Symporters; Thiogalactosides	1995
Ligand-induced conformational changes in the lactose permease of Escherichia coli: evidence for two binding sites. Protein science : a publication of the Protein Society, 1994, Volume: 3, Issue:12 Topics: Amino Acid Sequence; Anilino Naphthalenesulfonates; Bacterial Proteins; Binding Sites; Coumarins; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Isopropyl Thiogalactoside; Lactose; Ligands; Membrane Transport Modulators; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Fusion Proteins; Spectrometry, Fluorescence; Spin Labels; Symporters; Thiogalactosides; Valine	1994
Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies. Biochemistry, 1994, Oct-11, Volume: 33, Issue:40 Topics: Anilino Naphthalenesulfonates; Base Sequence; Binding Sites; Cysteine; Escherichia coli; Escherichia coli Proteins; Galactose; Lactose; Ligands; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Mutation; Protein Structure, Secondary; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Reagents; Symporters; Trisaccharides	1994
Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry, 1996, Sep-10, Volume: 35, Issue:36 Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acid Sequence; Anilino Naphthalenesulfonates; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Binding Sites; Binding, Competitive; Biological Transport; CHO Cells; Cricetinae; Cysteine; Drug Resistance, Multiple; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Ethylmaleimide; Fluorescent Dyes; Kinetics; Molecular Sequence Data; Nucleotides; Spectrometry, Fluorescence; Sulfhydryl Reagents	1996
Movement of a loop in domain 3 of aerolysin is required for channel formation. Biochemistry, 1998, Jan-13, Volume: 37, Issue:2 Topics: Aeromonas; Anilino Naphthalenesulfonates; Bacterial Toxins; Biological Assay; Crystallography, X-Ray; Cysteine; Fluorescent Dyes; Ion Channels; Models, Molecular; Movement; Mutagenesis, Site-Directed; Pore Forming Cytotoxic Proteins; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Tryptophan	1998
Conformational changes at the highly reactive cystein and lysine regions of skeletal muscle myosin induced by formation of transition state analogues. Journal of biochemistry, 1998, Volume: 124, Issue:3 Topics: Adenosine Triphosphatases; Anilino Naphthalenesulfonates; Animals; Chickens; Cysteine; Lysine; Muscle, Skeletal; Myosins; Picrates; Protein Conformation; Spectrometry, Fluorescence; Sulfhydryl Reagents	1998
Zinc stabilizes the SecB binding site of SecA. Biochemistry, 1999, Apr-20, Volume: 38, Issue:16 Topics: Adenosine Triphosphatases; Amino Acid Sequence; Anilino Naphthalenesulfonates; Bacterial Proteins; Binding Sites; Biological Transport; Cations, Divalent; Chelating Agents; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylenediamines; Membrane Transport Proteins; Molecular Chaperones; Molecular Sequence Data; Peptide Fragments; SEC Translocation Channels; SecA Proteins; Sulfhydryl Reagents; Zinc	1999
The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labeling. The Journal of biological chemistry, 1999, Jul-02, Volume: 274, Issue:27 Topics: Amino Acid Sequence; Anilino Naphthalenesulfonates; Cell Membrane; Cysteine; Escherichia coli; Fluorescent Dyes; Molecular Sequence Data; NADP Transhydrogenases; Oxadiazoles; Proton Pumps; Sulfhydryl Reagents; Ultraviolet Rays	1999
Cys(577) is a conformationally mobile residue in the ATP-binding domain of the Na,K-ATPase alpha-subunit. The Journal of biological chemistry, 1999, Aug-27, Volume: 274, Issue:35 Topics: Adenosine Triphosphate; Anilino Naphthalenesulfonates; Binding Sites; Cations; Chromatography, High Pressure Liquid; Cysteine; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Kinetics; Peptide Fragments; Protein Binding; Sequence Analysis; Sodium-Potassium-Exchanging ATPase; Trypsin	1999
Expression of an active Na,K-ATPase with an alpha-subunit lacking all twenty-three native cysteine residues. The Journal of biological chemistry, 2000, Sep-29, Volume: 275, Issue:39 Topics: Adenosine Triphosphate; Anilino Naphthalenesulfonates; Animals; Baculoviridae; Cysteine; Enzyme Inhibitors; Kidney; Models, Molecular; Mutation; Ouabain; Potassium Chloride; Sheep; Sodium Chloride; Sodium-Potassium-Exchanging ATPase; Spodoptera; Sulfhydryl Reagents	2000
Binding of spin-labeled galactosides to the lactose permease of Escherichia coli. Biochemistry, 2000, Sep-19, Volume: 39, Issue:37 Topics: Alkylating Agents; Anilino Naphthalenesulfonates; Binding Sites; Biological Transport; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Galactose; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Protein Structure, Secondary; Pyrrolidines; Spin Labels; Spin Trapping; Symporters; Thiogalactosides	2000
Identification of a region involved in the communication between the NADP(H) binding domain and the membrane domain in proton pumping E. coli transhydrogenase. Biochemistry, 2001, Aug-21, Volume: 40, Issue:33 Topics: Amino Acid Sequence; Anilino Naphthalenesulfonates; Cell Membrane; Cysteine; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Magnesium Chloride; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NADP; NADP Transhydrogenases; Plasmids; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Proteolipids; Protons; Spectrometry, Fluorescence; Time Factors	2001
The essential role of a free sulfhydryl group in blocking the cholesteryl site of cholesteryl ester transfer protein (CETP). Chemistry and physics of lipids, 2002, Volume: 114, Issue:2 Topics: 2-Naphthylamine; Amino Acid Sequence; Anilino Naphthalenesulfonates; Binding Sites; Biological Transport, Active; Carrier Proteins; Cholesterol Ester Transfer Proteins; Cholesterol Esters; Cysteine; Ethylmaleimide; Glycoproteins; In Vitro Techniques; Kinetics; Molecular Sequence Data; Peptide Fragments; Recombinant Proteins; Spectrometry, Fluorescence; Sulfhydryl Compounds	2002
A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability. Biochemistry, 2003, Mar-18, Volume: 42, Issue:10 Topics: Amino Acid Substitution; Anilino Naphthalenesulfonates; Binding Sites; Cysteine; Escherichia coli Proteins; Gene Expression Regulation; Glycine; Hot Temperature; Ligands; Maltose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Insertional; Protein Conformation; Protein Transport; Substrate Specificity; Symporters; Thermodynamics	2003
Nucleotide and phospholipid-dependent control of PPXD and C-domain association for SecA ATPase. Biochemistry, 2003, Nov-25, Volume: 42, Issue:46 Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Amino Acid Substitution; Anilino Naphthalenesulfonates; Bacillus subtilis; Bacterial Proteins; Cysteine; Escherichia coli Proteins; Fluorescence Resonance Energy Transfer; Membrane Transport Proteins; Models, Molecular; Phospholipids; Protein Structure, Tertiary; Recombinant Proteins; SEC Translocation Channels; SecA Proteins; Temperature; Tryptophan	2003
The relationship between MRP1 activities and its NBD conformational changes. Science in China. Series C, Life sciences, 2004, Volume: 47, Issue:5 Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Anilino Naphthalenesulfonates; Animals; Cell Line; Cesium; Cricetinae; Cysteine; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescence Resonance Energy Transfer; Humans; Hydrolysis; Models, Chemical; Multidrug Resistance-Associated Proteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Time Factors	2004
Interhelical packing modulates conformational flexibility in the lactose permease of Escherichia coli. Biochemistry, 2005, May-31, Volume: 44, Issue:21 Topics: Amino Acid Substitution; Anilino Naphthalenesulfonates; Biological Transport, Active; Catalysis; Cysteine; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Glycine; Hot Temperature; Intracellular Fluid; Lactose; Membrane Transport Modulators; Membrane Transport Proteins; Models, Molecular; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Symporters; Thermodynamics	2005
Sugar recognition by CscB and LacY. Biochemistry, 2011, Dec-27, Volume: 50, Issue:51 Topics: Alkylation; Anilino Naphthalenesulfonates; Binding Sites; Binding, Competitive; Biological Transport; Cysteine; Disaccharides; Escherichia coli; Escherichia coli Proteins; Fructose; Galactosides; Glucosides; Glycosides; Kinetics; Lactulose; Membrane Transport Proteins; Models, Molecular; Molecular Conformation; Monosaccharide Transport Proteins; Recombinant Proteins; Sulfhydryl Reagents; Symporters	2011