fructose-1,6-diphosphate has been researched along with guanosine diphosphate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Gross, M; Rubino, MS; Starn, TK | 1 |
| Singh, LP; Wahba, AJ | 1 |
| Byrnes, M; Chang, SH; Younathan, ES; Zhu, X | 1 |
| Borza, T; Fromm, HJ; Honzatko, RB; Iancu, CV; Pike, E | 1 |
4 other study(ies) available for fructose-1,6-diphosphate and guanosine diphosphate
| Article | Year |
|---|---|
Regulation of protein synthesis in rabbit reticulocyte lysate. Glucose 6-phosphate is required to maintain the activity of eukaryotic initiation factor (eIF)-2B by a mechanism that is independent of the phosphorylation of eIF-2 alpha.
Topics: Animals; Chromatography, Gel; Cyclic AMP; Cycloheximide; eIF-2 Kinase; Eukaryotic Initiation Factor-2; Fructosediphosphates; Glucose-6-Phosphate; Glucosephosphates; Guanosine Diphosphate; Guanosine Triphosphate; Hemin; Immunoglobulin G; Isocitrates; Kinetics; Peptide Initiation Factors; Phosphorylation; Protein Biosynthesis; Protein Kinases; Protein Synthesis Inhibitors; Proteins; Rabbits; Reticulocytes | 1988 |
Allosteric activation of rabbit reticulocyte guanine nucleotide exchange factor activity by sugar phosphates and inositol phosphates.
Topics: Allosteric Regulation; Animals; Fructosediphosphates; Guanine Nucleotide Exchange Factors; Guanosine Diphosphate; Guanosine Triphosphate; Inositol Phosphates; Proteins; Rabbits; Reticulocytes | 1995 |
Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Binding Sites; Binding, Competitive; Fructosediphosphates; Fructosephosphates; Geobacillus stearothermophilus; Guanosine Diphosphate; Kinetics; Mutagenesis, Site-Directed; Phosphofructokinase-1; Structure-Activity Relationship | 1994 |
Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance.
Topics: Adenosine Monophosphate; Adenylosuccinate Synthase; Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Dimerization; DNA, Complementary; Dose-Response Relationship, Drug; Enzyme Inhibitors; Escherichia coli; Fructosediphosphates; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Kinetics; Ligands; Mice; Models, Chemical; Models, Molecular; Molecular Sequence Data; Protein Isoforms; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Temperature; Ultracentrifugation | 2003 |