4-nitrophenylmaltoside has been researched along with glucose, (beta-d)-isomer in 14 studies
| Studies (4-nitrophenylmaltoside) | Trials (4-nitrophenylmaltoside) | Recent Studies (post-2010) (4-nitrophenylmaltoside) | Studies (glucose, (beta-d)-isomer) | Trials (glucose, (beta-d)-isomer) | Recent Studies (post-2010) (glucose, (beta-d)-isomer) |
|---|---|---|---|---|---|
| 15 | 0 | 2 | 21,956 | 883 | 10,747 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (28.57) | 18.7374 |
| 1990's | 5 (35.71) | 18.2507 |
| 2000's | 3 (21.43) | 29.6817 |
| 2010's | 2 (14.29) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Abe, J; Ajandouz, EH; Marchis-Mouren, G; Svensson, B | 1 |
| Ikenaka, T; Matsubara, K; Omichi, K; Shiosaki, K | 1 |
| Aubry, C; Dupuy, G; Hilaire, G | 1 |
| Reyes, M; Shuman, HA; Treptow, NA | 1 |
| Ikenaka, T; Omichi, K | 1 |
| Müller-Matthesius, R | 1 |
| Nakatani, H; Tonomura, B; Yamashita, H | 1 |
| Lanskaya, IM; Lukomskaya, IS; Podkidisheva, EI; Voznyi, YV | 1 |
| Hemavathy, KC; Levine, MJ; Miyamoto, M; Ramalingam, K; Ramasubbu, N; Tseng, CC | 1 |
| Payan, F; Qian, M; Zhuo, H | 1 |
| Fuseda, N; Hayashi, M; Mizuma, T | 1 |
| Cafarella, T; Crouch, E; Head, J; McDonald, B; Seaton, B; Smith, K | 1 |
| Ahn, HJ; Kim, JH; Kim, YW; Li, C | 1 |
| Chaudhuri, TK; Equbal, MJ; Malik, ST; Pastor, A; Shukla, PK; Singh, AK; Singh, TP | 1 |
14 other study(ies) available for 4-nitrophenylmaltoside and glucose, (beta-d)-isomer
| Article | Year |
|---|---|
Barley malt-alpha-amylase. Purification, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates.
Topics: alpha-Amylases; Electrophoresis, Polyacrylamide Gel; Glucose; Glucosides; Hordeum; Isoelectric Focusing; Isoenzymes; Oligosaccharides; Substrate Specificity | 1992 |
Differentiation of human non-salivary, non-pancreatic alpha-amylase from salivary and pancreatic alpha-amylases by use of FG5P.
Topics: alpha-Amylases; Binding Sites; Carbohydrate Sequence; Glucosides; Glycosides; Humans; Hydrogen-Ion Concentration; Hydrolysis; Molecular Sequence Data; Nitrobenzenes; Oligosaccharides; Pancreas; Saliva; Substrate Specificity; Yeasts | 1990 |
Rapid determination of alpha-amylase activity by use of a new chromogenic substrate.
Topics: alpha-Amylases; alpha-Glucosidases; Glucan 1,4-alpha-Glucosidase; Glucosides; Humans; Hydrogen-Ion Concentration; Nitrophenols; Pancreas; Saliva | 1987 |
Transport of p-nitrophenyl-alpha-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic alpha-maltosidase.
Topics: alpha-Glucosidases; ATP-Binding Cassette Transporters; Biological Transport; Carrier Proteins; Cytoplasm; Enzyme Induction; Escherichia coli; Escherichia coli Proteins; Genes; Genes, Bacterial; Glucosidases; Glucosides; Glycosides; Kinetics; Maltose-Binding Proteins; Monosaccharide Transport Proteins; Nitrophenols; Periplasmic Binding Proteins | 1986 |
Differential rate assay of human pancreatic and salivary alpha-amylases in serum using two coupled enzymes.
Topics: alpha-Amylases; alpha-Glucosidases; Glucosides; Glycoside Hydrolases; Humans; Kinetics; Oligo-1,6-Glucosidase; Pancreas; Saccharomyces; Saccharomyces cerevisiae; Saliva | 1986 |
[Amylase determination using p-nitrophenylmaltosides].
Topics: Amylases; Glucosides; Glycosides; Humans; Indicators and Reagents | 1982 |
Effect of a p-nitro group of phenyl-maltooligosaccharide substrate on the change of action specificity of lysine-modified porcine pancreatic alpha-amylase.
Topics: alpha-Amylases; Animals; Glucose; Glucosides; Kinetics; Lysine; Maltose; Nitrobenzenes; Oligosaccharides; Pancreas; Structure-Activity Relationship; Substrate Specificity; Swine; Trisaccharides | 1995 |
Use of beta-maltosides (p-nitrophenyl-beta-D-maltoside, 2-chloro-4- nitrophenyl-beta-D-maltoside and 4-methylumbelliferyl-beta-D-maltoside) as substrates for the assay of neutral alpha-glucosidase from human kidney and urine.
Topics: Acetylglucosaminidase; alpha-Galactosidase; Automation; Glucosides; Humans; Hymecromone; Kidney; Kidney Transplantation; Kinetics; Maltose; Microvilli; Nitrobenzenes; Sensitivity and Specificity; Spectrophotometry; Substrate Specificity | 1996 |
The roles of histidine residues at the starch-binding site in streptococcal-binding activities of human salivary amylase.
Topics: Alanine; alpha-Amylases; Bacterial Adhesion; Binding Sites; DNA, Viral; Escherichia coli; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Genetic Vectors; Glucans; Glucosides; Histidine; Humans; Hydrolysis; Mutagenesis, Site-Directed; Mutation; Oligosaccharides; Saliva; Starch; Streptococcus | 1999 |
Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site.
Topics: alpha-Amylases; Animals; Aspartic Acid; Binding Sites; Carbohydrate Sequence; Carbohydrates; Catalysis; Catalytic Domain; Crystallography, X-Ray; Electrons; Fourier Analysis; Glucosides; Hydrogen Bonding; Hydrolysis; Ligands; Molecular Sequence Data; Pancreas; Protein Conformation; Swine; Temperature; X-Rays | 2004 |
Kinetic characterization of glycosidase activity from disaccharide conjugate to monosaccharide conjugate in Caco-2 cells.
Topics: Caco-2 Cells; Glucosides; Glycoside Hydrolases; Glycosides; Humans; Hydrolysis; Kinetics | 2005 |
Contributions of phenylalanine 335 to ligand recognition by human surfactant protein D: ring interactions with SP-D ligands.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Crystallography; Evolution, Molecular; Glucosides; Humans; Hydrophobic and Hydrophilic Interactions; Indoles; Leucine; Ligands; Molecular Sequence Data; Phenylalanine; Protein Binding; Protein Structure, Tertiary; Pulmonary Surfactant-Associated Protein D; Structure-Activity Relationship; Trisaccharides | 2006 |
Transglycosylation of engineered cyclodextrin glucanotransferases as O-glycoligases.
Topics: Alanine; Escherichia coli; Gene Expression; Glucosides; Glucosyltransferases; Glutamic Acid; Glycosylation; Kinetics; Ligases; Mutagenesis, Site-Directed; Mutation; Protein Engineering; Serine | 2014 |
Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein.
Topics: Amino Acid Sequence; Binding Sites; Chaperonin 60; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Gene Expression; Glucosides; Glycoside Hydrolases; Models, Molecular; Protein Aggregates; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Folding; Protein Interaction Domains and Motifs; Recombinant Proteins; Sequence Alignment; Structural Homology, Protein; Substrate Specificity | 2016 |