4-nitrophenylgalactoside has been researched along with galactose in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bhat, N; Joe, A; PereiraPerrin, M; Ward, HD | 1 |
| Amyes, TL; Heo, C; Huber, RE; Lin, S; Richard, JP | 1 |
| Gunawan, P; Kaback, HR; Lawrence, MC; Sahin-Tóth, M; Toyokuni, T | 1 |
| Feinberg, H; Lansky, S; Salama, R; Shoham, G; Shoham, Y; Solomon, HV; Tabachnikov, O | 1 |
4 other study(ies) available for 4-nitrophenylgalactoside and galactose
| Article | Year |
|---|---|
Cryptosporidium p30, a galactose/N-acetylgalactosamine-specific lectin, mediates infection in vitro.
Topics: Acetylgalactosamine; Amino Acid Sequence; Animals; Caco-2 Cells; Chromatography, Affinity; Cryptosporidiosis; Cryptosporidium; Cryptosporidium parvum; Escherichia coli; Galactose; Glycoproteins; Humans; Lectins; Molecular Sequence Data; Monosaccharides; Open Reading Frames; Sporozoites | 2007 |
Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 4. Mechanism for reaction of nucleophiles with the galactosyl-enzyme intermediates of E461G and E461Q beta-galactosidases.
Topics: Acetates; Azides; beta-Galactosidase; Escherichia coli; Formates; Galactose; Galactosides; Kinetics; Models, Chemical; Nitrophenylgalactosides; Point Mutation; Structure-Activity Relationship; Water | 1996 |
Binding of hydrophobic D-galactopyranosides to the lactose permease of Escherichia coli.
Topics: Binding Sites; Calcium-Binding Proteins; Chemical Phenomena; Chemistry, Physical; Escherichia coli; Escherichia coli Proteins; Galactose; Hydrophobic and Hydrophilic Interactions; Membrane Transport Proteins; Methylgalactosides; Monosaccharide Transport Proteins; Nitrophenylgalactosides; Periplasmic Binding Proteins; Symporters; Thiogalactosides | 2002 |
Structure-function relationships in Gan42B, an intracellular GH42 β-galactosidase from Geobacillus stearothermophilus.
Topics: Amino Acid Sequence; Bacterial Proteins; beta-Galactosidase; Catalytic Domain; Crystallography, X-Ray; Escherichia coli; Galactose; Gene Expression; Geobacillus stearothermophilus; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Nitrophenylgalactosides; Oligosaccharides; Protein Binding; Protein Multimerization; Protein Structure, Secondary; Protein Subunits; Recombinant Proteins; Sequence Alignment; Structural Homology, Protein; Structure-Activity Relationship | 2015 |