The DOI matches its Crossref record; 275 of the 275 references it cites were found in a registry or an index.
Protein Kinases and Phosphatases in the Control of Cell Fate
Open accessAbstract
Protein phosphorylation controls many aspects of cell fate and is often deregulated in pathological conditions. Several recent findings have provided an intriguing insight into the spatial regulation of protein phosphorylation across different subcellular compartments and how this can be finely orchestrated by specific kinases and phosphatases. In this review, the focus will be placed on (i) the phosphoinositide 3-kinase (PI3K) pathway, specifically on the kinases Akt and mTOR and on the phosphatases PP2a and PTEN, and on (ii) the PKC family of serine/threonine kinases. We will look at general aspects of cell physiology controlled by these kinases and phosphatases, highlighting the signalling pathways that drive cell division, proliferation, and apoptosis.
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Cites
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
AKT/PKB signaling: navigating downstream
Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115
Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Li, J., Yen, C., Liaw, D., Podsypanina, K., Bose, S., Wang, S. I., Puc, J., Miliaresis, C., Rodgers, L., McCombie, R., et al. (1997) · Science · doi:10.1126/science.275.5308.1943 · Cited by 4,785
Intracellular Signaling by Hydrolysis of Phospholipids and Activation of Protein Kinase C
Nishizuka, Y. (1992) · Science · doi:10.1126/science.1411571 · Cited by 4,472
High Frequency of Mutations of the PIK3CA Gene in Human Cancers
Samuels, Y., Wang, Z., Bardelli, A., Silliman, N., Ptak, J., Szabo, S., Yan, H., Gazdar, A., Powell, S. M., Riggins, G. J., et al. (2004) · Science · doi:10.1126/science.1096502 · Cited by 3,437
The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
Engelman, J. A., Luo, J., & Cantley, L. C. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1879 · Cited by 3,330
Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104
Mechanism of activation of protein kinase B by insulin and IGF-1.
Alessi, D. R., Andjelkovic, M., Caudwell, B., Cron, P., Morrice, N., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,004
Cited by
ERK1/2 MAP kinases: Structure, function, and regulation
Roskoski, R. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,650
Roskoski, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2015.10.021 · Cited by 886
Protein phosphatase 2A: a target for anticancer therapy
Perrotti, D., & Neviani, P. (2013) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70558-2 · Cited by 400
Targeting ERK1/2 protein-serine/threonine kinases in human cancers
Roskoski, R. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.01.039 · Cited by 308
Physiopathology of the Permeability Transition Pore: Molecular Mechanisms in Human Pathology
Bonora, M., Patergnani, S., Ramaccini, D., Morciano, G., Pedriali, G., Kahsay, A., Bouhamida, E., Giorgi, C., Wieckowski, M., & Pinton, P. (2020) · Biomolecules · doi:10.3390/biom10070998 · Cited by 135
Self-citation
Metadata
- Authors
- Bononi, A., Agnoletto, C., De Marchi, E., Marchi, S., Patergnani, S., Bonora, M., Giorgi, C., Missiroli, S., Poletti, F., Rimessi, A., & Pinton, P.
- Venue
- Enzyme Research
- Publisher
- Hindawi Limited
- Published
- 2011-09-04
- Volume
- 2011
- Pages
- 1-26
- ISSN
- 2090-0406 (ISSN-L)
- 2090-0414
- OpenAlex
- W2145817798
- Cited by
- 285
- References
- 275
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- diamond
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- Bononi, A., Agnoletto, C., De Marchi, E., Marchi, S., Patergnani, S., Bonora, M., Giorgi, C., Missiroli, S., Poletti, F., Rimessi, A., & Pinton, P. (2011). Protein Kinases and Phosphatases in the Control of Cell Fate. Enzyme Research. https://doi.org/10.4061/2011/329098
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