The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The TORrid affairs of viruses: effects of mammalian DNA viruses on the PI3K–Akt–mTOR signalling pathway
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Citations
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
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
Brugarolas, J., Lei, K., Hurley, R. L., Manning, B. D., Reiling, J. H., Hafen, E., Witters, L. A., Ellisen, L. W., & Kaelin, W. G. (2004) · Genes & Development · doi:10.1101/gad.1256804 · Cited by 1,384
Rheb Binds and Regulates the mTOR Kinase
Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., & Avruch, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.053 · Cited by 1,005
mTOR, translation initiation and cancer
Mamane, Y., Petroulakis, E., LeBacquer, O., & Sonenberg, N. (2006) · Oncogene · doi:10.1038/sj.onc.1209888 · Cited by 607
Arsham, A. M., Howell, J. J., & Simon, M. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212770200 · Cited by 463
AMPK, the metabolic syndrome and cancer
Luo, Z., Saha, A. K., Xiang, X., & Ruderman, N. B. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.12.011 · Cited by 426
Rheb Activates mTOR by Antagonizing Its Endogenous Inhibitor, FKBP38
Bai, X., Ma, D., Liu, A., Shen, X., Wang, Q. J., Liu, Y., & Jiang, Y. (2007) · Science · doi:10.1126/science.1147379 · Cited by 382
Growth Control Under Stress: mTOR Regulation through the REDD1-TSC Pathway
Ellisen, L. W. (2005) · Cell Cycle · doi:10.4161/cc.4.11.2139 · Cited by 131
Cited by
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Sonenberg, N., & Hinnebusch, A. G. (2009) · Cell · doi:10.1016/j.cell.2009.01.042 · Cited by 3,304
“Stimulation of eIF4F assembly is caused in part by the activation of the PI3K/Akt/mTOR pathway, which results in phosphorylation of 4E-BPs through different mechanisms (Buchkovich et al., 2008).”
Regulation of Ligands for the NKG2D Activating Receptor
Raulet, D. H., Gasser, S., Gowen, B. G., Deng, W., & Jung, H. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-095951 · Cited by 848
Why do viruses cause cancer? Highlights of the first century of human tumour virology
Moore, P. S., & Chang, Y. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2961 · Cited by 745
Viruses, microRNAs, and Host Interactions
Skalsky, R. L., & Cullen, B. R. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134243 · Cited by 676
The Akt–SREBP nexus: cell signaling meets lipid metabolism
Krycer, J. R., Sharpe, L. J., Luu, W., & Brown, A. J. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2010.01.001 · Cited by 360
Metadata
- Authors
- Buchkovich, N. J., Yu, Y., Zampieri, C. A., & Alwine, J. C.
- Venue
- Nature Reviews Microbiology
- Published
- 2008-03-03
- Volume
- 6
- Issue
- 4
- Pages
- 266-275
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W2075059034
- Cited by
- 229
- References
- 9
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- green
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
