lactose has been researched along with 4-nitrophenylgalactoside in 12 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (16.67) | 18.7374 |
| 1990's | 5 (41.67) | 18.2507 |
| 2000's | 3 (25.00) | 29.6817 |
| 2010's | 2 (16.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kaback, HR; Lee, J; Patel, L; Persson, B; Roepe, PD | 1 |
| Cupples, CG; Huber, RE; Miller, JH | 1 |
| Anraku, Y; Yamato, I | 1 |
| Kaback, HR; Roepe, PD | 1 |
| Driessen, AJ; Kaback, HR; Konings, WN; Lolkema, JS; van Iwaarden, PR | 1 |
| Schnuch, M; Seebauer, H | 1 |
| Kaback, HR; Kharabi, D; le Coutre, J; le Maire, G; Lee, JC; Sahin-Tóth, M | 1 |
| Kaback, HR; Sahin-Toth, M | 1 |
| Guan, L; Hu, Y; Kaback, HR | 1 |
| Cheng, C; Cupples, CG; Edwards, RA; Hakda, S; Huber, RE | 1 |
| Gänzle, MG; Schwab, C; Sørensen, KI | 1 |
| Andersson, M; Chau, BT; Jiang, X; Kaback, HR; Villafuerte, MK; Wong, LY | 1 |
12 other study(ies) available for lactose and 4-nitrophenylgalactoside
| Article | Year |
|---|---|
Site-directed mutagenesis of lysine 319 in the lactose permease of Escherichia coli.
Topics: Affinity Labels; Biological Transport, Active; Diffusion; Escherichia coli; Escherichia coli Proteins; Hydrogen-Ion Concentration; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Structure-Activity Relationship; Symporters | 1992 |
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 |
Dependence on pH of substrate binding to a mutant lactose carrier, lacYun, in Escherichia coli. A model for H+/lactose symport.
Topics: Binding Sites; Biological Transport, Active; Cloning, Molecular; Escherichia coli; Genes, Bacterial; Hydrogen-Ion Concentration; Lactose; Models, Biological; Mutation; Nitrophenylgalactosides; Protons | 1989 |
Site-directed mutagenesis of tyrosine residues in the lac permease of Escherichia coli.
Topics: Amino Acid Sequence; Base Sequence; Biological Transport, Active; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Lactose; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutation; Nitrophenylgalactosides; Protein Conformation; Symporters; Tyrosine | 1989 |
Exchange, efflux, and substrate binding by cysteine mutants of the lactose permease of Escherichia coli.
Topics: Amino Acid Sequence; Binding Sites; Cysteine; Escherichia coli; Escherichia coli Proteins; Hydrogen-Ion Concentration; Kinetics; Lactose; Liposomes; Membrane Transport Proteins; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis; Nitrophenylgalactosides; Structure-Activity Relationship; Symporters | 1993 |
Sugar cell responses to lactose and sucrose in labellar and tarsal taste hairs of Musca domestica.
Topics: Animals; Carbohydrates; Chemoreceptor Cells; Drug Combinations; Electrophysiology; Female; Houseflies; Lactose; Male; Nitrophenylgalactosides; Sucrose; Taste | 1998 |
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 |
Aromatic stacking in the sugar binding site of the lactose permease.
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 |
Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer.
Topics: Amino Acid Substitution; beta-Galactosidase; Binding Sites; Binding, Competitive; Catalysis; Enzyme Activation; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Kinetics; Lac Operon; Lactose; Nitrophenylgalactosides; Protein Binding; Sequence Deletion; Thermodynamics; Tryptophan | 2003 |
Heterologous expression of glycoside hydrolase family 2 and 42 β-galactosidases of lactic acid bacteria in Lactococcus lactis.
Topics: Bacterial Proteins; Cloning, Molecular; Enzyme Stability; Gene Expression; Glycoside Hydrolases; Hydrogen-Ion Concentration; Kinetics; Lactobacillus acidophilus; Lactobacillus plantarum; Lactococcus lactis; Lactose; Leuconostoc; Nitrophenylgalactosides; Recombinant Proteins; Streptococcus thermophilus; Substrate Specificity; Temperature | 2010 |
Role of Conserved Gly-Gly Pairs on the Periplasmic Side of LacY.
Topics: Alkylation; Amino Acid Sequence; Amino Acid Substitution; Biological Transport, Active; Conserved Sequence; Escherichia coli; Escherichia coli Proteins; Glycylglycine; Lactose; Models, Molecular; Molecular Dynamics Simulation; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Periplasm; Protein Conformation; Protein Conformation, alpha-Helical; Symporters | 2016 |