Structural basis for allosteric regulation of human phosphofructokinase-1
Author:
Funder
U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences
West Virginia University Start-up funding
Czech Science Foundation
Publisher
Springer Science and Business Media LLC
Link
https://www.nature.com/articles/s41467-024-51808-6.pdf
Reference71 articles.
1. Evans, P. R., Farrants, G. W. & Lawrence, M. C. Crystallographic structure of allosterically inhibited phosphofructokinase at 7 A resolution. J. Mol. Biol. 191, 713–720 (1986).
2. Schirmer, T. & Evans, P. R. Structural basis of the allosteric behaviour of phosphofructokinase. Nature 343, 140–145 (1990).
3. Evans, P. R., Farrants, G. W. & Hudson, P. J. Phosphofructokinase: structure and control. Philos. Trans. R. Soc. Lond. B Biol. Sci. 293, 53–62 (1981).
4. Poorman, R. A., Randolph, A., Kemp, R. G. & Heinrikson, R. L. Evolution of phosphofructokinase—gene duplication and creation of new effector sites. Nature 309, 467–469 (1984).
5. Kemp, R. G. & Gunasekera, D. Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase. Biochemistry 41, 9426–9430 (2002).
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