Compounds > 4-nitrophenylgalactoside
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4-nitrophenylgalactoside and ethylmaleimide

4-nitrophenylgalactoside has been researched along with ethylmaleimide in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (66.67)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Brabetz, W; Liebl, W; Schleifer, KH1
Kaback, HR; Kharabi, D; le Coutre, J; le Maire, G; Lee, JC; Sahin-Tóth, M1
Guan, L; Hu, Y; Kaback, HR1

Other Studies

3 other study(ies) available for 4-nitrophenylgalactoside and ethylmaleimide

ArticleYear
Lactose permease of Escherichia coli catalyzes active beta-galactoside transport in a gram-positive bacterium.
    Journal of bacteriology, 1993, Volume: 175, Issue:22

    Topics: beta-Galactosidase; Biological Transport; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Carrier Proteins; Cell Membrane; Corynebacterium; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Genes, Bacterial; Kinetics; Membrane Transport Proteins; Mercuric Chloride; Methylgalactosides; Monosaccharide Transport Proteins; Nitrophenylgalactosides; Recombination, Genetic; Symporters; Thiogalactosides

1993
Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli.
    Biochemistry, 1999, Jan-12, Volume: 38, Issue:2

    Topics: Amino Acid Substitution; Arginine; Binding Sites; Biological Transport, Active; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Glutamic Acid; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protons; Substrate Specificity; Symporters; Thiogalactosides

1999
Aromatic stacking in the sugar binding site of the lactose permease.
    Biochemistry, 2003, Feb-18, Volume: 42, Issue:6

    Topics: Alkylation; Amino Acids, Aromatic; Binding Sites; Biological Transport, Active; Cysteine; Escherichia coli Proteins; Ethylmaleimide; Kinetics; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Nitrophenylgalactosides; Phenylalanine; Substrate Specificity; Symporters; Thiogalactosides; Tryptophan; Tyrosine

2003