acebutolol has been researched along with phenylalanine in 16 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (25.00) | 18.7374 |
| 1990's | 4 (25.00) | 18.2507 |
| 2000's | 4 (25.00) | 29.6817 |
| 2010's | 2 (12.50) | 24.3611 |
| 2020's | 2 (12.50) | 2.80 |
| Authors | Studies |
|---|---|
| Bellman, K; Knegtel, RM; Settimo, L | 1 |
| Brenner, L; Ritter, RC; Yox, DP | 1 |
| Ritter, RC; Stokesberry, H; Yox, DP | 2 |
| Closs, O; Digranes, A | 1 |
| Iwata, M; Nishijima, M | 1 |
| Caplow, M; Heizer, WD; Shoaf, CR | 1 |
| Frank, ME; Hettinger, TP; MacKinnon, BI; Rehnberg, BG | 1 |
| Andersen, C; Benz, R; Orlik, F | 1 |
| Christensen, T; Frandsen, TP; Kaarsholm, NC; Sigurskjold, BW; Svensson, B | 1 |
| CAMPBELL, LL; WELKER, NE | 1 |
| Kwak, EJ; Lim, SI | 1 |
| Adachi, M; Hirata, A; Mikami, B; Utsumi, S | 1 |
| Kim, YM; Kimura, A; Mori, H; Nakai, H; Okuyama, M; Svensson, B; Tagami, T; Taguchi, K | 1 |
| Hao, N; Jie, C; Li, J; Liu, Z; Wu, B | 1 |
| Chen, R; Dai, L; Ni, G; Wang, F; Xia, C; Zhang, L; Zhao, Y; Zhong, L | 1 |
16 other study(ies) available for acebutolol and phenylalanine
| Article | Year |
|---|---|
Comparison of the accuracy of experimental and predicted pKa values of basic and acidic compounds.
Topics: Chemistry, Pharmaceutical; Forecasting; Hydrogen-Ion Concentration; Pharmaceutical Preparations; Random Allocation | 2014 |
CCK-receptor antagonists attenuate suppression of sham feeding by intestinal nutrients.
Topics: Amylases; Animal Nutritional Physiological Phenomena; Animals; Benzodiazepinones; Catheterization; Cholecystokinin; Devazepide; Duodenum; Eating; Intestines; Male; Maltose; Oleic Acid; Oleic Acids; Phenylalanine; Proglumide; Rats; Rats, Inbred Strains; Receptors, Cholecystokinin; Satiety Response; Sincalide; Stomach | 1992 |
Vagotomy attenuates suppression of sham feeding induced by intestinal nutrients.
Topics: Animal Nutritional Physiological Phenomena; Animals; Cholecystokinin; Eating; Injections; Intestinal Mucosa; Intestines; Male; Maltose; Oleic Acid; Oleic Acids; Phenylalanine; Rats; Rats, Inbred Strains; Sincalide; Sucrose; Vagotomy | 1991 |
Fourth ventricular capsaicin attenuates suppression of sham feeding induced by intestinal nutrients.
Topics: Animals; Capsaicin; Cerebral Ventricles; Eating; Food; Injections, Intraventricular; Intestines; Male; Maltose; Peritoneum; Phenylalanine; Rats; Rats, Inbred Strains; Rhombencephalon; Satiation; Sincalide; Sucrose | 1991 |
Rapid identification of Proteus species and Providencia by a simple two-step procedure.
Topics: Bacteriological Techniques; Carboxy-Lyases; Culture Media; Enterobacteriaceae; Fermentation; Galactosidases; Hydrogen Sulfide; Maltose; Methods; Ornithine; Phenylalanine; Proteus; Proteus mirabilis; Proteus vulgaris; Urease | 1973 |
[Effects of maltose infusion on amino acid composition of maternal venous blood and fetal blood in utero].
Topics: Adult; Amino Acids; Aspartic Acid; Blood Glucose; Female; Fetal Blood; Humans; Infusions, Parenteral; Maltose; Maternal-Fetal Exchange; Phenylalanine; Pregnancy | 1983 |
Uptake of the components of phenylalanylphenylalanine and maltose by intestinal epithelium.
Topics: Animals; Biological Transport; Dipeptides; Epithelium; Glucose Oxidase; In Vitro Techniques; Intestinal Absorption; Intestine, Small; Kinetics; Maltose; Phenylalanine; Rats; Sodium | 1980 |
Taste qualities of solutions preferred by hamsters.
Topics: Animals; Behavior, Animal; Chorda Tympani Nerve; Cluster Analysis; Cricetinae; Cyclamates; Electrophysiology; Glossopharyngeal Nerve; Male; Maltose; Mesocricetus; Molecular Structure; Phenylalanine; Phenylurea Compounds; Saccharin; Sucrose; Sweetening Agents; Taste | 1999 |
Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli. II. Effect on maltose and maltooligosaccharide binding kinetics.
Topics: Bacterial Outer Membrane Proteins; Biological Transport; Biophysical Phenomena; Biophysics; Carbohydrate Metabolism; Carbohydrates; Crystallography, X-Ray; Escherichia coli; Glucans; Kinetics; Lipid Bilayers; Lipids; Maltose; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oligosaccharides; Phenylalanine; Porins; Protein Binding; Receptors, Virus; Time Factors; Trisaccharides; Tryptophan; Tyrosine | 2002 |
Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger.
Topics: Amino Acid Substitution; Aspartic Acid; Aspergillus niger; Binding Sites; Calorimetry; Glucan 1,4-alpha-Glucosidase; Glucans; Guanidine; Kinetics; Maltose; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Sequence Deletion; Substrate Specificity; Tryptophan; Valine | 2002 |
PREFERENTIAL SYNTHESIS OF ALPHA-AMYLASE BY BACILLUS STEAROTHERMOPHILUS IN THE PRESENCE OF 5-METHYL-TRYPTOPHAN.
Topics: alpha-Amylases; Amylases; Antimetabolites; Bacillus; Bacteriological Techniques; Geobacillus stearothermophilus; Maltose; Metabolism; Phenylalanine; Proline; Proteins; Research; Tryptophan | 1964 |
The effect of sugar, amino acid, metal ion, and NaCl on model Maillard reaction under pH control.
Topics: Alanine; Amino Acids; Arabinose; Arginine; Aspartic Acid; Biochemistry; Carbohydrates; Colorimetry; Copper; Cysteine; Fructose; Glucose; Glutamic Acid; Glycine max; Hot Temperature; Hydrogen-Ion Concentration; Ions; Iron; Isoleucine; Leucine; Lysine; Maltose; Metals; Models, Chemical; Phenylalanine; Proline; Serine; Sodium Chloride; Temperature; Time Factors; Valine; Xylose | 2004 |
Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type.
Topics: Asparagine; Bacillus cereus; Bacterial Proteins; beta-Amylase; Binding Sites; Crystallography, X-Ray; Enzyme Activation; Glutamic Acid; Glycine max; Hydrogen-Ion Concentration; Kinetics; Maltose; Methionine; Mutagenesis, Site-Directed; Phenylalanine; Plant Proteins; Threonine; Tyrosine | 2004 |
Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates.
Topics: alpha-Glucosidases; Amino Acid Substitution; Aspergillus niger; Fungal Proteins; Maltose; Mutation, Missense; Oligosaccharides; Phenylalanine; Protein Structure, Secondary; Sequence Alignment; Substrate Specificity | 2013 |
A multifunctional α-amylase BSGH13 from Bacillus subtilis BS-5 possessing endoglucanase and xylanase activities.
Topics: alpha-Amylases; Amino Acid Substitution; Bacillus subtilis; Bacterial Proteins; Catalytic Domain; Cellulase; Cellulose; Cloning, Molecular; Endo-1,4-beta Xylanases; Escherichia coli; Gene Expression; Genetic Vectors; Kinetics; Maltose; Models, Molecular; Mutation; Phenylalanine; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Recombinant Proteins; Structural Homology, Protein; Structure-Activity Relationship; Substrate Specificity; Tetroses; Tryptophan; Xylans | 2021 |
Phenylalanine 314 is essential for the activity of maltogenic amylase from Corallococcus sp. EGB.
Topics: Coma; Humans; Hydrolysis; Kinetics; Maltose; Myxococcales; Phenylalanine; Starch; Substrate Specificity | 2022 |