Inhibition of phosphofructokinase by fructose 1,6-diphosphatase in mammalian systems: Protein-protein interaction or fructose 1,6-diphosphate trapping?☆
References (9)
- et al.
J. Biol. Chem
(1974) - et al.
Arch. Biochem. Biophys
(1975) - et al.
J. Biol. Chem
(1974) - et al.
J. Biol. Chem
(1965)
There are more references available in the full text version of this article.
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This work was supported by a grant from the Deutsche Forschungsgemeinschaft to H. D. Söling.
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