Compounds > thiodigalactoside
Page last updated: 2024-09-03

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

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

Compound Research Comparison

Studies
(thiodigalactoside)		Trials
(thiodigalactoside)		Recent Studies (post-2010)
(thiodigalactoside)		Studies
(2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid)		Trials
(2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid)		Recent Studies (post-2010) (2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid)
740246902

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Frillingos, S; Kaback, HR; Wu, J1
Frillingos, S; Kaback, HR; Voss, J; Wu, J1
He, MM; Kaback, HR1
Kaback, HR; Kasho, V; Smirnova, IN1

Other Studies

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

ArticleYear
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
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
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