Compounds > lactose
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lactose and 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid

lactose has been researched along with 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (57.14)18.2507
2000's3 (42.86)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Frillingos, S; Kaback, HR; Voss, J; Wu, J1
Kaback, HR; Wu, J1
Consler, TG; Kaback, HR; Weitzman, C1
He, MM; Kaback, HR1
Altenbach, C; Hideg, K; Hubbell, WL; Kaback, HR; Kálai, T; Zhao, M1
Ermolova, NV; Kaback, HR; Kasho, VN; Smirnova, IN1
Kaback, HR; Kasho, V; Smirnova, IN1

Other Studies

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

ArticleYear
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
Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: structural properties and evidence for a substrate-induced conformational change.
    Protein science : a publication of the Protein Society, 1995, Volume: 4, Issue:11

    Topics: Acrylamide; Acrylamides; Amino Acid Sequence; Anilino Naphthalenesulfonates; Escherichia coli; Escherichia coli Proteins; Iodides; Lactose; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Reagents; Symporters; Tryptophan

1995
Interaction between residues Glu269 (helix VIII) and His322 (helix X) of the lactose permease of Escherichia coli is essential for substrate binding.
    Biochemistry, 1997, Nov-04, Volume: 36, Issue:44

    Topics: Anilino Naphthalenesulfonates; Biotinylation; Escherichia coli; Escherichia coli Proteins; Galactose; Glutamine; Histidine; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Binding; Protein Structure, Secondary; Substrate Specificity; Sulfhydryl Reagents; Symporters; Thiogalactosides

1997
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
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
Protonation and sugar binding to LacY.
    Proceedings of the National Academy of Sciences of the United States of America, 2008, Jul-01, Volume: 105, Issue:26

    Topics: Anilino Naphthalenesulfonates; Biological Transport; Carbohydrate Metabolism; Escherichia coli; Fluorescence; Hydrogen-Ion Concentration; Kinetics; Lactose; Maleimides; Melibiose; Membrane Transport Proteins; Nitrophenylgalactosides; Protein Structure, Secondary; Protons; Thiogalactosides

2008