 Fructose-Bisphosphate Aldolase
"Fructose-Bisphosphate Aldolase" 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.
An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13.
| Descriptor ID |
D005634
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| MeSH Number(s) |
D08.811.520.224.062.400
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| Concept/Terms |
Fructose-Bisphosphate Aldolase- Fructose-Bisphosphate Aldolase
- Aldolase, Fructose-Bisphosphate
- Fructose Bisphosphate Aldolase
- Fructose 1,6-Bisphosphate Aldolase
- 1,6-Bisphosphate Aldolase, Fructose
- Aldolase, Fructose 1,6-Bisphosphate
- Fructose 1,6 Bisphosphate Aldolase
- Fructose Biphosphate Aldolase
- Aldolase, Fructose Biphosphate
- Fructosediphosphate Aldolase
- Aldolase, Fructosediphosphate
- Aldolase
- Fructose 1,6-Bisphosphate Aldolase, Class II
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Below are MeSH descriptors whose meaning is more general than "Fructose-Bisphosphate Aldolase".
Below are MeSH descriptors whose meaning is more specific than "Fructose-Bisphosphate Aldolase".
This graph shows the total number of publications written about "Fructose-Bisphosphate Aldolase" by people in this website by year, and whether "Fructose-Bisphosphate Aldolase" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1980 | 0 | 1 | 1 | | 1981 | 1 | 0 | 1 | | 1984 | 1 | 0 | 1 | | 1999 | 1 | 0 | 1 | | 2002 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 |
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Below are the most recent publications written about "Fructose-Bisphosphate Aldolase" by people in Profiles.
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Grifone R, Laclef C, Spitz F, Lopez S, Demignon J, Guidotti JE, Kawakami K, Xu PX, Kelly R, Petrof BJ, Daegelen D, Concordet JP, Maire P. Six1 and Eya1 expression can reprogram adult muscle from the slow-twitch phenotype into the fast-twitch phenotype. Mol Cell Biol. 2004 Jul; 24(14):6253-67.
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Spitz F, Benbacer L, Sabourin JC, Salminen M, Chen F, Cywiner C, Kahn A, Chatelet F, Maire P, Daegelen D. Fiber-type specific and position-dependent expression of a transgene in limb muscles. Differentiation. 2002 Oct; 70(8):457-67.
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Spitz F, Demignon J, Kahn A, Daegelen D, Maire P. Developmental regulation of the aldolase A muscle-specific promoter during in vivo muscle maturation is controlled by a nuclear receptor binding element. J Mol Biol. 1999 Jun 18; 289(4):893-903.
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Jenkins JD, Madden DP, Steck TL. Association of phosphofructokinase and aldolase with the membrane of the intact erythrocyte. J Biol Chem. 1984 Aug 10; 259(15):9374-8.
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Murthy SN, Liu T, Kaul RK, Köhler H, Steck TL. The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3. J Biol Chem. 1981 Nov 10; 256(21):11203-8.
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Kliman HJ, Steck TL. Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane. A kinetic analysis. J Biol Chem. 1980 Jul 10; 255(13):6314-21.
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Rice WR, Steck TL. Pyruvate transport into inside-out vesicles isolated from human erythrocyte membranes. Biochim Biophys Acta. 1977 Jul 14; 468(2):305-17.
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Strapazon E, Steck TL. Interaction of the aldolase and the membrane of human erythrocytes. Biochemistry. 1977 Jun 28; 16(13):2966-71.
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Strapazon E, Steck TL. Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membrane. Biochemistry. 1976 Apr 06; 15(7):1421-4.
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Szuchet S, Yphantis DA. Equilibrium sedimentation of proteins in acid solutions. Dissociation of aldolase by aqueous acetic acid. Biochemistry. 1973 Dec 04; 12(25):5115-27.
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