arginine and thiodigalactoside

arginine has been researched along with thiodigalactoside in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Brooker, RJ; Eelkema, JA; Franco, PJ	1
Kaback, HR; Kharabi, D; le Coutre, J; le Maire, G; Lee, JC; Sahin-Tóth, M	1

Other Studies

2 other study(ies) available for arginine and thiodigalactoside

Article	Year
Isolation and characterization of thiodigalactoside-resistant mutants of the lactose permease which possess an enhanced recognition for maltose. The Journal of biological chemistry, 1989, Sep-25, Volume: 264, Issue:27 Topics: Arginine; Base Sequence; Biological Transport, Active; Codon; Drug Resistance, Microbial; Escherichia coli; Escherichia coli Proteins; Maltose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutation; Plasmids; Protein Binding; Substrate Specificity; Symporters; Thiogalactosides; Thioglycosides	1989
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

Article

Year

Isolation and characterization of thiodigalactoside-resistant mutants of the lactose permease which possess an enhanced recognition for maltose.

The Journal of biological chemistry, 1989, Sep-25, Volume: 264, Issue:27

Topics: Arginine; Base Sequence; Biological Transport, Active; Codon; Drug Resistance, Microbial; Escherichia coli; Escherichia coli Proteins; Maltose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutation; Plasmids; Protein Binding; Substrate Specificity; Symporters; Thiogalactosides; Thioglycosides

1989

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