The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Mammalian target of rapamycin inhibition as therapy for hematologic malignancies
Abstract
The mammalian target of rapamycin (mTOR) is a downstream effector of the phosphatidylinositol 3‐kinase (PI3K)/Akt (protein kinase B) signaling pathway, which mediates cell survival and proliferation. mTOR regulates essential signal‐transduction pathways, is involved in the coupling of growth stimuli with cell cycle progression, and initiates mRNA translation in response to favorable nutrient environments. mTOR is involved in regulating many aspects of cell growth, including membrane traffic, protein degradation, protein kinase C signaling, ribosome biogenesis, and transcription. Because mTOR activates both the 40S ribosomal protein S6 kinase (p70s6k) and the eukaryotic initiation factor 4E‐binding protein 1, its inhibitors cause G 1‐phase cell cycle arrest. Inhibitors of mTOR also prevent cyclin dependent kinase (CDK) activation, inhibit retinoblastoma protein phosphorylation, and accelerate the turnover of cyclin D1, leading to a deficiency of active CDK4/cyclin D1 complexes, all of which may help cause G 1‐phase arrest. It is known that the phosphatase and tensin homologue tumor suppressor gene (PTEN) plays a major role in embryonic development, cell migration, and apoptosis. Malignancies with PTEN mutations, which are associated with constitutive activation of the PI3K/Akt pathway, are relatively resistant to apoptosis and may be particularly sensitive to mTOR inhibitors. Rapamycin analogs with relatively favorable pharmaceutical properties, including CCI‐779, RAD001, and AP23573, are under investigation in patients with hematologic malignancies. Cancer 2004;100:657–66. © 2004 American Cancer Society.
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Cites
Principles of interleukin (IL)-6-type cytokine signalling and its regulation
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“Cytokines, including interleukin-6 and IGF-1, support the growth and prevent the apoptosis of malignant plasma cells.(79) – 83 In the bone marrow, it has been shown that cytokines activate PI3K in myeloma cells.”
BackgroundTSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545
Rapamycin suppresses 5′TOP mRNA translation through inhibition of p70s6k
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Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells
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“Loss of TSC1/TSC2 results in mTOR dependent increase in kinase activity of p70S6K, a serine-threonine kinase, and confers resistance of cells to amino-acid starvation.32 Conversely, coexpression of TSC1 and TSC2 inhibits activation of S6K1 in nutrient-deprived cells.33 Evidence that TSC1/TSC2 lies upstream of mTOR com…”
BackgroundPhosphorylation and Activation of p70 s6k by PDK1
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RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.
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Cited by
Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB
Sarbassov, D. D., Ali, S. M., Sengupta, S., Sheen, J.-H., Hsu, P. P., Bagley, A. F., Markhard, A. L., & Sabatini, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.029 · Cited by 2,365
Vigneri, P., Frasca, F., Sciacca, L., Pandini, G., & Vigneri, R. (2009) · Endocrine Related Cancer · doi:10.1677/erc-09-0087 · Cited by 1,009
Sirolimus for Kaposi's Sarcoma in Renal-Transplant Recipients
Stallone, G., Schena, A., Infante, B., Di Paolo, S., Loverre, A., Maggio, G., Ranieri, E., Gesualdo, L., Schena, F. P., & Grandaliano, G. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa042831 · Cited by 990
Contributions of the Raf/MEK/ERK, PI3K/PTEN/Akt/mTOR and Jak/STAT pathways to leukemia
Steelman, L. S., Abrams, S. L., Whelan, J., Bertrand, F. E., Ludwig, D. E., Bäsecke, J., Libra, M., Stivala, F., Milella, M., Tafuri, A., et al. (2008) · Leukemia · doi:10.1038/leu.2008.26 · Cited by 385
Rapamycin derivatives reduce mTORC2 signaling and inhibit AKT activation in AML
Zeng, Z., Sarbassov, D. D., Samudio, I. J., Yee, K. W. L., Munsell, M. F., Ellen Jackson, C., Giles, F. J., Sabatini, D. M., Andreeff, M., & Konopleva, M. (2007) · Blood · doi:10.1182/blood-2006-06-030833 · Cited by 342
Self-citation
Metadata
- Authors
- Panwalkar, A., Verstovsek, S., & Giles, F. J.
- Venue
- Cancer
- Publisher
- Wiley
- Published
- 2004-02-03
- Volume
- 100
- Issue
- 4
- Pages
- 657-666
- ISSN
- 0008-543X (ISSN-L)
- 1097-0142
- OpenAlex
- W2008932991
- Cited by
- 208
- References
- 9
- FWCI
- 9.73
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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