4-nitrophenylgalactoside has been researched along with glutamic acid in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (66.67) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cupples, CG; Huber, RE; Miller, JH | 1 |
| Kaback, HR; Kharabi, D; le Coutre, J; le Maire, G; Lee, JC; Sahin-Tóth, M | 1 |
| Kaback, HR; Sahin-Toth, M | 1 |
3 other study(ies) available for 4-nitrophenylgalactoside and glutamic acid
| Article | Year |
|---|---|
Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.
Topics: beta-Galactosidase; Binding Sites; Drug Stability; Edetic Acid; Escherichia coli; Galactosidases; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Lactose; Mutation; Nitrophenylgalactosides; Ribose; Structure-Activity Relationship | 1990 |
Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli.
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 |
Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli.
Topics: Arginine; Biological Transport; Biological Transport, Active; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis; Nitrophenylgalactosides; Protons; Substrate Specificity; Symporters | 2001 |