"Fructosediphosphates" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Diphosphoric acid esters of fructose. The fructose-1,6- diphosphate isomer is most prevalent. It is an important intermediate in the glycolysis process.
| Descriptor ID |
D005635
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| MeSH Number(s) |
D09.894.417.313.300 D09.894.417.592.300
|
| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Fructosediphosphates".
Below are MeSH descriptors whose meaning is more specific than "Fructosediphosphates".
This graph shows the total number of publications written about "Fructosediphosphates" by people in this website by year, and whether "Fructosediphosphates" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 1 | 1 | 2 |
| 1999 | 0 | 2 | 2 |
| 2006 | 0 | 1 | 1 |
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Below are the most recent publications written about "Fructosediphosphates" by people in Profiles.
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GC-MS metabolic profiling reveals fructose-2,6-bisphosphate regulates branched chain amino acid metabolism in the heart during fasting. Metabolomics. 2019 01 28; 15(2):18.
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Optimum activity of the phosphofructokinase from Ascaris suum requires more than one metal ion. Biochemistry. 2006 Feb 21; 45(7):2453-60.
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Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated. Arch Biochem Biophys. 1999 May 15; 365(2):335-43.
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Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities. J Biol Chem. 1999 Jan 22; 274(4):2176-84.
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A pH-dependent allosteric transition in Ascaris suum phosphofructokinase distinct from that observed with fructose 2,6-bisphosphate. Arch Biochem Biophys. 1995 Oct 01; 322(2):410-6.
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Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase. Biochemistry. 1995 Jun 20; 34(24):7781-7.
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Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state. Biochemistry. 1991 Oct 15; 30(41):9998-10004.
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Fructose 2,6-bisphosphate and AMP increase the affinity of the Ascaris suum phosphofructokinase for fructose 6-phosphate in a process separate from the relief of ATP inhibition. J Biol Chem. 1991 May 15; 266(14):8891-6.
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Kinetic studies on the activation of pyrophosphate-dependent phosphofructokinase from mung bean by fructose 2,6-bisphosphate and related compounds. Biochemistry. 1986 Aug 12; 25(16):4682-7.