glucosamine 6-phosphate has been researched along with glutaminase in 3 studies
| Studies (glucosamine 6-phosphate) | Trials (glucosamine 6-phosphate) | Recent Studies (post-2010) (glucosamine 6-phosphate) | Studies (glutaminase) | Trials (glutaminase) | Recent Studies (post-2010) (glutaminase) |
|---|---|---|---|---|---|
| 124 | 0 | 47 | 2,301 | 11 | 738 |
| Protein | Taxonomy | glucosamine 6-phosphate (IC50) | glutaminase (IC50) |
|---|---|---|---|
| Protein-glutamine gamma-glutamyltransferase 2 | Homo sapiens (human) | 0.045 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Broschat, KO; Davies, MS; Gorka, C; Gulve, EA; Huang Hc, HC; Kasten, TP; Martin-Berger, CL; Page, JD; Salsgiver, WJ | 1 |
| Aïssi, E; Bouquelet, S; Brassart, C; Foley, S; Krzewinski, F; Mouni, F; Stolarczyk, E; Vidal, O | 1 |
| Badet-Denisot, MA; Golinelli-Pimpaneau, B; Mouilleron, S | 1 |
3 other study(ies) available for glucosamine 6-phosphate and glutaminase
| Article | Year |
|---|---|
Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: potent feedback inhibition by glucosamine 6-phosphate.
Topics: Animals; Cell Line; Enzyme Inhibitors; Enzyme Stability; Glucosamine; Glucose-6-Phosphate; Glutaminase; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Humans; Kinetics | 2002 |
Characterisation of glutamine fructose-6-phosphate amidotransferase (EC 2.6.1.16) and N-acetylglucosamine metabolism in Bifidobacterium.
Topics: Acetylglucosamine; Amino Acid Sequence; Bacterial Proteins; Bifidobacterium; Catalytic Domain; Cloning, Molecular; Conserved Sequence; Enzyme Stability; Escherichia coli; Fructosephosphates; Gene Expression; Glucosamine; Glucose-6-Phosphate; Glutamic Acid; Glutaminase; Glutamine; Hydrogen-Ion Concentration; Metabolic Networks and Pathways; Models, Biological; Molecular Sequence Data; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Temperature | 2008 |
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel.
Topics: Ammonia; Carbohydrates; Catalytic Domain; Crystallography, X-Ray; Cyclization; Escherichia coli; Glucosamine; Glucose-6-Phosphate; Glutaminase; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Models, Molecular; Protein Folding; Protein Structure, Tertiary; Solvents | 2008 |