Compounds > 4-nitrophenylgalactoside
Page last updated: 2024-08-24

4-nitrophenylgalactoside and isopropyl thiogalactoside

4-nitrophenylgalactoside has been researched along with isopropyl thiogalactoside in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's1 (33.33)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Janda, KD; Lerner, RA; Lo, CH; Lo, LC; Sim, MM; Wang, R; Wong, CH1
Cámara, M; Diggle, SP; Dodd, C; Stacey, RE; Williams, P; Winzer, K1
Fraser, ME; Huber, RE; Jancewicz, LJ; Lee, M; Sutendra, G; Wheatley, RW1

Other Studies

3 other study(ies) available for 4-nitrophenylgalactoside and isopropyl thiogalactoside

ArticleYear
Chemical selection for catalysis in combinatorial antibody libraries.
    Science (New York, N.Y.), 1997, Feb-14, Volume: 275, Issue:5302

    Topics: Animals; Antibodies, Catalytic; beta-Galactosidase; Catalysis; Cloning, Molecular; Coliphages; Dithiothreitol; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Galactosides; Haptens; Hybridomas; Immunoglobulin Fab Fragments; Indoles; Isopropyl Thiogalactoside; Mice; Nitrophenylgalactosides; Peptide Library; Polymerase Chain Reaction; Serum Albumin, Bovine; Transformation, Bacterial

1997
The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa.
    Environmental microbiology, 2006, Volume: 8, Issue:6

    Topics: Adhesins, Bacterial; Biofilms; Environment, Controlled; Glycosides; Isopropyl Thiogalactoside; Nitrophenylgalactosides; Polystyrenes; Pseudomonas aeruginosa; Signal Transduction; Stainless Steel

2006
Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.
    Archives of biochemistry and biophysics, 2012, Jan-15, Volume: 517, Issue:2

    Topics: Amino Acid Substitution; beta-Galactosidase; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Isopropyl Thiogalactoside; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Conformation; Recombinant Proteins; Serine; Static Electricity

2012