4-nitrophenylgalactoside has been researched along with glucose, (beta-d)-isomer in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (50.00) | 18.2507 |
2000's | 1 (16.67) | 29.6817 |
2010's | 2 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Fukumura, M; Ohmiya, K; Sakka, K; Shimada, K | 1 |
Awazu, S; Hayashi, M; Mizuma, T; Ohta, K | 1 |
Akao, T; Hattori, M; Kobashi, K; Yang, L | 1 |
Hengstenberg, W; Schulte, D | 1 |
Cao, A; Liu, Y; Tang, Y | 1 |
Ashfaq, UA; Ehsan, B; Haq, A; Idrees, S; Rajoka, MI | 1 |
6 other study(ies) available for 4-nitrophenylgalactoside and glucose, (beta-d)-isomer
Article | Year |
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Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an extremely thermostable xylanase, and characterization of the translated product.
Topics: Amino Acid Sequence; Base Sequence; beta-Glucosidase; Clostridium; Electrophoresis, Polyacrylamide Gel; Enzyme Stability; Escherichia coli; Gene Expression Regulation, Enzymologic; Glucosides; Glycoside Hydrolases; Glycosides; Hot Temperature; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Nitrophenylgalactosides; Promoter Regions, Genetic; Protein Biosynthesis; Restriction Mapping; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Substrate Specificity; Xylan Endo-1,3-beta-Xylosidase; Xylosidases | 1995 |
Comparative study of active absorption by the intestine and disposition of anomers of sugar-conjugated compounds.
Topics: Animals; Biological Transport; Glucosides; Intestinal Absorption; Male; Nitrophenylgalactosides; Prodrugs; Rats; Rats, Wistar; Time Factors | 1993 |
A sennoside-hydrolyzing beta-glucosidase from Bifidobacterium sp. strain SEN is inducible.
Topics: Anthraquinones; beta-Glucosidase; Bifidobacterium; Chloramphenicol; Enzyme Induction; Feces; Glucose; Glucosides; Humans; Nitrophenylgalactosides; RNA, Bacterial; Senna Extract; Sennosides; Substrate Specificity | 1996 |
Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis.
Topics: Amino Acid Substitution; Amino Acids; Bacterial Proteins; beta-Galactosidase; Binding Sites; Escherichia coli; Galactosephosphates; Glucosides; Glycoside Hydrolases; Lactococcus lactis; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Structure, Tertiary; Recombinant Fusion Proteins; Species Specificity; Substrate Specificity | 2000 |
Novel fluorescent biosensor for α-glucosidase inhibitor screening based on cationic conjugated polymers.
Topics: alpha-Glucosidases; Biosensing Techniques; Cations; Diabetes Mellitus; Fluorenes; Fluorescent Dyes; Glucosides; Humans; Hydrolysis; Inhibitory Concentration 50; Kinetics; Nitrophenols; Nitrophenylgalactosides; Polymers; Quaternary Ammonium Compounds; Spectrophotometry | 2012 |
Determination of substrate specificities against β-glucosidase A (BglA) from Thermotoga maritime: a molecular docking approach.
Topics: Amino Acid Sequence; Benzyl Alcohols; beta-Glucosidase; Cellobiose; Glucosides; Hydrogen Bonding; Hymecromone; Kinetics; Molecular Conformation; Molecular Docking Simulation; Nitrophenylgalactosides; Software; Substrate Specificity; Thermotoga maritima | 2015 |