lactose has been researched along with allolactose in 17 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 7 (41.18) | 18.7374 |
| 1990's | 1 (5.88) | 18.2507 |
| 2000's | 2 (11.76) | 29.6817 |
| 2010's | 7 (41.18) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Huber, RE; Kurz, G; Wallenfels, K | 1 |
| Huber, RE; Turner, CL | 1 |
| Mahaffy, JM | 2 |
| Huber, RE; Hurlburt, KL; Turner, CL | 1 |
| Hall, BG | 1 |
| Bahl, H; Huber, RE; Roth, NJ | 1 |
| Cheng, C; Cupples, CG; Edwards, RA; Hakda, S; Huber, RE | 1 |
| LESPAGNOL, A; MONTREUIL, J; SEGARD, E | 1 |
| Fairbanks, BM; Maheshwari, A; Matthews, KS; Swint-Kruse, L; Zhan, H | 1 |
| Chen, M; Liu, S; Ma, J; Matthews, KS; Xu, J | 1 |
| Huber, RE; Juers, DH; Matthews, BW | 1 |
| Ballesteros, AO; Fernandez-Arrojo, L; Illanes, A; Plou, FJ; Rodriguez-Colinas, B; Urrutia, P; Wilson, L | 1 |
| Dugdale, ML; Huber, RE; Jancewicz, LJ; Lo, S; Wheatley, RW | 1 |
| Boom, RM; Janssen, AE; Jia, W; Paudel, E; Warmerdam, A | 1 |
| Arreola, SL; Haltrich, D; Intanon, M; Kittl, R; Kosma, P; Nguyen, TH; Pham, NH; Suljic, J | 1 |
| Huber, RE; Wheatley, RW | 1 |
1 review(s) available for lactose and allolactose
| Article | Year |
|---|---|
LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance.
Topics: Animals; beta-Galactosidase; Galactose; Humans; Lactose; Models, Molecular; Protein Conformation; Substrate Specificity | 2012 |
16 other study(ies) available for lactose and allolactose
| Article | Year |
|---|---|
The action of beta-galactosidase (Escherichia coli) on allolactose.
Topics: Escherichia coli; Galactosidases; Hydrogen-Ion Concentration; Isomerism; Kinetics; Lactose | 1975 |
Differential binding of allolactose anomers to the lactose repressor of Escherichia coli.
Topics: Binding, Competitive; Escherichia coli; Genes, Regulator; Isopropyl Thiogalactoside; Lactose; Operon; Stereoisomerism | 1977 |
Cellular control models with linked positive and negative feedback and delays. II. Linear analysis and local stability.
Topics: Computers; Escherichia coli; Feedback; Lac Operon; Lactose; Mathematics; Models, Genetic; Repressor Proteins | 1984 |
Cellular control models with linked positive and negative feedback and delays. I. The models.
Topics: Escherichia coli; Feedback; Kinetics; Lac Operon; Lactose; Mathematics; Models, Genetic; Repressor Proteins; Transcription, Genetic | 1984 |
The anomeric specificity of beta-galactosidase and lac permease from Escherichia coli.
Topics: beta-Galactosidase; Escherichia coli; Escherichia coli Proteins; Galactosidases; Glucose; Kinetics; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Nitrophenylgalactosides; Stereoisomerism; Substrate Specificity; Symporters | 1981 |
Transgalactosylation activity of ebg beta-galactosidase synthesizes allolactose from lactose.
Topics: beta-Galactosidase; Enzyme Induction; Escherichia coli; Galactose; Galactosidases; Glucose; Kinetics; Lac Operon; Lactose | 1982 |
Quaternary structure, Mg2+ interactions, and some kinetic properties of the beta-galactosidase from Thermoanaerobacterium thermosulfurigenes EM1.
Topics: Bacteria, Anaerobic; beta-Galactosidase; Binding, Competitive; Dialysis; Dimerization; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Enzyme Stability; Escherichia coli; Galactosides; Glucose; Hydrogen-Ion Concentration; Kinetics; Lactose; Magnesium; Methanol; Potassium; Protein Conformation; Sodium; Substrate Specificity | 1996 |
Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer.
Topics: Amino Acid Substitution; beta-Galactosidase; Binding Sites; Binding, Competitive; Catalysis; Enzyme Activation; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Kinetics; Lac Operon; Lactose; Nitrophenylgalactosides; Protein Binding; Sequence Deletion; Thermodynamics; Tryptophan | 2003 |
[The problem of "allolactose" of human milk].
Topics: Disaccharides; Humans; Lactose; Milk, Human | 1960 |
Perturbation from a distance: mutations that alter LacI function through long-range effects.
Topics: Amino Acid Substitution; Bacterial Proteins; DNA-Binding Proteins; Escherichia coli Proteins; Isopropyl Thiogalactoside; Lac Repressors; Lactose; Melibiose; Mutagenesis, Site-Directed; Operator Regions, Genetic; Phenotype; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Repressor Proteins; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea | 2003 |
Altering residues N125 and D149 impacts sugar effector binding and allosteric parameters in Escherichia coli lactose repressor.
Topics: Allosteric Regulation; Amino Acid Substitution; Asparagine; Aspartic Acid; DNA-Binding Proteins; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Glycosides; Lac Operon; Lac Repressors; Lactose; Ligands; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Protein Multimerization | 2011 |
Detailed analysis of galactooligosaccharides synthesis with β-galactosidase from Aspergillus oryzae.
Topics: Aspergillus oryzae; Bacillus; beta-Galactosidase; Disaccharides; Hydrogen-Ion Concentration; Kluyveromyces; Lactose; Magnetic Resonance Spectroscopy; Temperature; Trisaccharides | 2013 |
Structural explanation for allolactose (lac operon inducer) synthesis by lacZ β-galactosidase and the evolutionary relationship between allolactose synthesis and the lac repressor.
Topics: Amino Acid Substitution; beta-Galactosidase; Binding Sites; Escherichia coli Proteins; Evolution, Molecular; Lac Repressors; Lactose; Mutation, Missense | 2013 |
Characterization of β-galactosidase isoforms from Bacillus circulans and their contribution to GOS production.
Topics: Bacillus; Bacterial Proteins; beta-Galactosidase; Catalytic Domain; Enzyme Activation; Galactose; Hydrolysis; Isoenzymes; Lactose; Molecular Weight; Thermodynamics; Trisaccharides | 2013 |
Two β-galactosidases from the human isolate Bifidobacterium breve DSM 20213: molecular cloning and expression, biochemical characterization and synthesis of galacto-oligosaccharides.
Topics: Bacterial Proteins; beta-Galactosidase; Bifidobacterium; Chaperonin 10; Chaperonin 60; Cloning, Molecular; Escherichia coli; Galactose; Gene Expression; Glucose; Humans; Hydrogen-Ion Concentration; Infant; Intestines; Isoenzymes; Kinetics; Lactose; Molecular Weight; Oligosaccharides; Protein Multimerization; Temperature | 2014 |
An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a (4)H3 conformation provides insights into the formation, conformation, and stabilization of the transition state.
Topics: Amino Acid Substitution; beta-Galactosidase; Binding Sites; Biocatalysis; Carbohydrate Conformation; Catalytic Domain; Computational Biology; Databases, Protein; Enzyme Stability; Escherichia coli Proteins; Histidine; Hydrogen Bonding; Lac Operon; Lactose; Models, Molecular; Mutation; Protein Conformation; Recombinant Proteins; Static Electricity; Stereoisomerism | 2015 |