fructose-6-phosphate has been researched along with manganese in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (20.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Mildvan, AS; Urbina, JA; Ysern, X | 1 |
Cronin, CN; Tipton, KF | 1 |
Bertagnolli, BL; Cook, PF | 1 |
Cheng, L; Zhou, R | 1 |
Akerboom, J; Baker, PJ; Berrisford, JM; Blackburn, GM; Brouns, S; Hardré, R; Murray, IA; Rice, DW; Salmon, L; Sedelnikova, SE; Turnbull, AP; van der Oost, J | 1 |
5 other study(ies) available for fructose-6-phosphate and manganese
Article | Year |
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Involvement of a divalent cation in the binding of fructose 6-phosphate to Trypanosoma cruzi phosphofructokinase: kinetic and magnetic resonance studies.
Topics: Animals; Cations, Divalent; Fructosephosphates; Kinetics; Magnesium; Magnetic Resonance Spectroscopy; Manganese; Mathematics; Phosphofructokinase-1; Trypanosoma cruzi | 1990 |
The roles of magnesium ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei.
Topics: Adenosine Triphosphate; Animals; Enzyme Activation; Fructosephosphates; Magnesium; Manganese; Phosphofructokinase-1; Trypanosoma brucei brucei | 1987 |
Lanthanide pyrophosphates as substrates for the pyrophosphate-dependent phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: evidence for a second metal ion required for reaction.
Topics: Binding Sites; Catalysis; Cations, Divalent; Cobalt; Fabaceae; Fructosephosphates; Magnesium; Manganese; Metals; Metals, Rare Earth; Phosphates; Phosphofructokinase-1; Plants, Medicinal; Propionibacterium; Substrate Specificity | 1994 |
Biochemical characterization of cytosolic fructose-1,6-bisphosphatase from apple (Malus domestica) leaves.
Topics: Adenosine Monophosphate; Binding, Competitive; Cytosol; Dihydroxyacetone Phosphate; Fructose; Fructose-Bisphosphatase; Fructosediphosphates; Fructosephosphates; Magnesium; Malus; Manganese; Molecular Structure; Molecular Weight; Plant Leaves; Sorbitol; Substrate Specificity; Sucrose | 2004 |
The structures of inhibitor complexes of Pyrococcus furiosus phosphoglucose isomerase provide insights into substrate binding and catalysis.
Topics: Archaeal Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Fructosephosphates; Glucose-6-Phosphate; Glucose-6-Phosphate Isomerase; Manganese; Models, Molecular; Molecular Structure; Pentosephosphates; Protein Binding; Protein Conformation; Pyrococcus furiosus | 2004 |