glucosamine 6-phosphate has been researched along with ammonium hydroxide in 3 studies
| Studies (glucosamine 6-phosphate) | Trials (glucosamine 6-phosphate) | Recent Studies (post-2010) (glucosamine 6-phosphate) | Studies (ammonium hydroxide) | Trials (ammonium hydroxide) | Recent Studies (post-2010) (ammonium hydroxide) |
|---|---|---|---|---|---|
| 124 | 0 | 47 | 29,152 | 577 | 9,136 |
| 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 |
|---|---|
| Badet, B; Badet-Denisot, MA; Leriche, C; Obmolova, G; Teplyakov, A | 1 |
| Badet, B; Badet-Denisot, MA; Daher, R; Floquet, N; Maigret, B; Mouilleron, S | 1 |
| Badet-Denisot, MA; Golinelli-Pimpaneau, B; Mouilleron, S | 1 |
1 review(s) available for glucosamine 6-phosphate and ammonium hydroxide
| Article | Year |
|---|---|
From Lobry de Bruyn to enzyme-catalyzed ammonia channelling: molecular studies of D-glucosamine-6P synthase.
Topics: Ammonia; Animals; Catalysis; Crystallography, X-Ray; Diabetes Mellitus, Type 2; Escherichia coli; Fungi; Glucosamine; Glucose; Glucose-6-Phosphate; Glutamine; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Humans; Hydrolysis; Mice; Molecular Structure; Nitrogen; Protein Conformation; Rats; Structure-Activity Relationship | 2002 |
2 other study(ies) available for glucosamine 6-phosphate and ammonium hydroxide
| Article | Year |
|---|---|
Ammonia channeling in bacterial glucosamine-6-phosphate synthase (Glms): molecular dynamics simulations and kinetic studies of protein mutants.
Topics: Ammonia; Bacterial Proteins; Binding Sites; Biological Transport; Computer Simulation; Crystallography, X-Ray; Escherichia coli; Glucosamine; Glucose-6-Phosphate; Glutamine; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Hydrolysis; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Point Mutation | 2007 |
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 |