The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Control of Glycolysis through Regulation of PFK1: Old Friends and Recent Additions
Open accessAbstract
Regulation of glucose metabolism is a crucial aspect of cell physiology in normal and disease conditions. Many regulatory events are involved in determining the metabolic fate of glucose and the pathways into which it is directed. The first reaction that commits glucose to the glycolytic pathway is catalyzed by the enzyme phosphofructokinase-1 (PFK-1) and is tightly regulated. One of the most potent activators of PFK-1 is fructose 2,6 bisphosphate (F2,6BP) and its cellular levels are correlated with glycolytic flux. F2,6BP is synthesized and degraded by a family of bifunctional enzymes-the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFB). The interplay among F2,6BP levels, the enzymes that generate and degrade it, and PFK-1 activity has important consequences for several different aspects of cell metabolism as well as for systemic metabolic conditions. TIGAR, a recently identified F2,6 bisphosphatase (F2,6BPase), could also contribute to this complexity and participate in shaping the metabolic profile of the cell.
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Almeida, A., Bolaños, J. P., & Moncada, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913668107 · Cited by 166
Moon, J.-S., Jin, W.-J., Kwak, J.-H., Kim, H.-J., Yun, M.-J., KIM, J.-W., Park, S. W., & Kim, K.-S. (2011) · Biochemical Journal · doi:10.1042/bj20101104 · Cited by 125
Regulation of 6-phosphofructo-1-kinase activity in ras-transformed rat-1 fibroblasts
Kole, H. K., Resnick, R. J., Van Doren, M., & Racker, E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90084-v · Cited by 57 · cited 2×
“Reciprocally, cells transformed by oncogenes such as v-src/vfps or ras showed elevated F2,6BP as well as increased glycolytic flux (Bosca et al. 1986; Kole et al. 1991), demonstrating the”
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Cited by
Everts, B., Amiel, E., Huang, S. C.-C., Smith, A. M., Chang, C.-H., Lam, W. Y., Redmann, V., Freitas, T. C., Blagih, J., van der Windt, G. J. W., et al. (2014) · Nature Immunology · doi:10.1038/ni.2833 · Cited by 1,064
Aerobic glycolysis tunes YAP/TAZ transcriptional activity
Enzo, E., Santinon, G., Pocaterra, A., Aragona, M., Bresolin, S., Forcato, M., Grifoni, D., Pession, A., Zanconato, F., Guzzo, G., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490379 · Cited by 414
Yang, Z., Fujii, H., Mohan, S. V., Goronzy, J. J., & Weyand, C. M. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20130252 · Cited by 334
Metabolic Basis of Creatine in Health and Disease: A Bioinformatics-Assisted Review
Bonilla, D. A., Kreider, R. B., Stout, J. R., Forero, D. A., Kerksick, C. M., Roberts, M. D., & Rawson, E. S. (2021) · Nutrients · doi:10.3390/nu13041238 · Cited by 223
Glycolytic reliance promotes anabolism in photoreceptors
Chinchore, Y., Begaj, T., Wu, D., Drokhlyansky, E., & Cepko, C. L. (2017) · eLife · doi:10.7554/elife.25946 · Cited by 191
Metadata
- Authors
- Mor, I., Cheung, E. C., & Vousden, K. H.
- Venue
- Cold Spring Harbor Symposia on Quantitative Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-01-01
- Volume
- 76
- Issue
- 0
- Pages
- 211-216
- ISSN
- 0091-7451 (ISSN-L)
- 1943-4456
- OpenAlex
- W2114104841
- Cited by
- 316
- References
- 3
- Type
- posted content
- Language
- en
- Open access
- bronze
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