Page last updated: 2024-08-24

4-nitrophenylgalactoside and thiodigalactoside

4-nitrophenylgalactoside has been researched along with thiodigalactoside in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Kaback, HR; Kharabi, D; le Coutre, J; le Maire, G; Lee, JC; Sahin-Tóth, M	1
Guan, L; Hu, Y; Kaback, HR	1

Other Studies

2 other study(ies) available for 4-nitrophenylgalactoside and thiodigalactoside

Article	Year
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

Article

Year

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