Compounds > 4-nitrophenyl alpha-glucoside
Page last updated: 2024-08-26

4-nitrophenyl alpha-glucoside and 4-nitrophenyl beta-d-glucoside

4-nitrophenyl alpha-glucoside has been researched along with 4-nitrophenyl beta-d-glucoside in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19901 (25.00)18.7374
1990's2 (50.00)18.2507
2000's0 (0.00)29.6817
2010's1 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Borel, JP; Cornillot, P; Gattegno, L; Gillery, P; Maquart, FX; Randoux, A1
Awazu, S; Hayashi, M; Mizuma, T; Ohta, K1
Christiansen, I; Hengstenberg, W1
Castillo, E; López-Munguía, A; Miranda-Molina, A; Saab-Rincón, G; Strompen, S1

Other Studies

4 other study(ies) available for 4-nitrophenyl alpha-glucoside and 4-nitrophenyl beta-d-glucoside

ArticleYear
A glucose-containing fraction extracted from the young erythrocyte membrane is capable of transferring glucose to hemoglobin in vitro.
    Diabetes, 1982, Volume: 31, Issue:4 Pt 1

    Topics: Erythrocyte Membrane; Erythrocytes; Glucose; Glucosides; Glycated Hemoglobin; Hemoglobin A; Hemoglobins; Humans; Isoelectric Focusing; Kinetics

1982
Comparative study of active absorption by the intestine and disposition of anomers of sugar-conjugated compounds.
    Biochemical pharmacology, 1993, Apr-06, Volume: 45, Issue:7

    Topics: Animals; Biological Transport; Glucosides; Intestinal Absorption; Male; Nitrophenylgalactosides; Prodrugs; Rats; Rats, Wistar; Time Factors

1993
Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system--two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?
    Microbiology (Reading, England), 1999, Volume: 145 ( Pt 10)

    Topics: Deoxyglucose; Enzyme Inhibitors; Glucose; Glucosides; Kinetics; Methylglucosides; Models, Biological; Multienzyme Complexes; Multigene Family; Mutagenesis, Site-Directed; Peptides; Phosphoenolpyruvate Sugar Phosphotransferase System; Promoter Regions, Genetic; Protein Engineering; Staphylococcus; Substrate Specificity

1999
Acceptor-induced modification of regioselectivity in CGTase-catalyzed glycosylations of p-nitrophenyl-glucopyranosides.
    Carbohydrate research, 2015, Mar-02, Volume: 404

    Topics: Bacillus; Bacterial Proteins; beta-Cyclodextrins; Catalysis; Glucosides; Glucosyltransferases; Glycosylation; Substrate Specificity; Thermoanaerobacter

2015