fructose-1,6-diphosphate has been researched along with tryptophan in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 1 (25.00) | 2.80 |
| Authors | Studies |
|---|---|
| Arora, S; Chaturvedi, A; Heuser, M; Joshi, G; Kumar, R; Patil, S | 1 |
| Rabinovitz, M | 1 |
| Deutscher, J; Di Pietro, A; Fieulaine, S; Galinier, A; Gonzalo, P; Jault, JM; Nessler, S | 1 |
| Galinier, A; Granet, Y; Grangeasse, C; Jault, JM; Lavergne, JP; Nessler, S; Pompeo, F | 1 |
1 review(s) available for fructose-1,6-diphosphate and tryptophan
| Article | Year |
|---|---|
The phosphofructokinase-uncharged tRNA interaction in metabolic and cell cycle control: an interpretive review.
Topics: Amino Acids; Animals; Cell Cycle; Cyclic AMP; Fructosediphosphates; Humans; In Vitro Techniques; Liver; Peptide Chain Initiation, Translational; Phosphofructokinase-1; RNA, Transfer; Signal Transduction; Tryptophan | 1995 |
3 other study(ies) available for fructose-1,6-diphosphate and tryptophan
| Article | Year |
|---|---|
A Perspective on Medicinal Chemistry Approaches for Targeting Pyruvate Kinase M2.
Topics: Allosteric Regulation; Allosteric Site; Carrier Proteins; Chemistry, Pharmaceutical; Glycolysis; Humans; Membrane Proteins; Protein Kinase Inhibitors; Thyroid Hormone-Binding Proteins; Thyroid Hormones | 2022 |
The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Bacillus subtilis; Bacterial Proteins; Binding, Competitive; Dose-Response Relationship, Drug; Fructosediphosphates; Iodides; Kinetics; Nucleotides; Phosphorylation; Protein Binding; Protein Conformation; Protein Serine-Threonine Kinases; Spectrometry, Fluorescence; Tryptophan; Ultracentrifugation | 2000 |
Regulation and mutational analysis of the HPr kinase/phosphorylase from Bacillus subtilis.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Sequence; Bacillus subtilis; Binding Sites; Fluorescence Resonance Energy Transfer; Fructosediphosphates; Kinetics; Magnesium; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphates; Phosphoprotein Phosphatases; Phosphorylation; Protein Serine-Threonine Kinases; Recombinant Proteins; Tryptophan | 2003 |