The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Upstream and downstream of mTOR
Open accessAbstract
The evolutionarily conserved checkpoint protein kinase, TOR (target of rapamycin), has emerged as a major effector of cell growth and proliferation via the regulation of protein synthesis. Work in the last decade clearly demonstrates that TOR controls protein synthesis through a stunning number of downstream targets. Some of the targets are phosphorylated directly by TOR, but many are phosphorylated indirectly. In this review, we summarize some recent developments in this fast-evolving field. We describe both the upstream components of the signaling pathway(s) that activates mammalian TOR (mTOR) and the downstream targets that affect protein synthesis. We also summarize the roles of mTOR in the control of cell growth and proliferation, as well as its relevance to cancer and synaptic plasticity.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“This pathway is an important regulator of cell proliferation and metabolism (Hay and Sonenberg, 2004; Guertin and Sabatini, 2007).”
From Efficient genetic editing of human intestinal organoids using ribonucleoprotein-based CRISPR (2023) · cites this paper as Hay and Sonenberg, 2004
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In the brain, mTORC1 tightly coordinates different synaptic plasticities -long-term potentiation (LTP) and long-term depression (LTD) -the molecular correlates of learning and memory (2)(3)(4)(5).”
From Analysis of proteins that rapidly change upon mechanistic/mammalian target of rapamycin complex 1 (mTORC1) repression identifies parkinson protein 7 (PARK7) as a novel protein aberrantly expressed in tuberous sclerosis complex (TSC) (2016) · cites this paper as [4]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Targeting HIF-1 for cancer therapy
Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., Oppliger, W., Jenoe, P., & Hall, M. N. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00636-6 · Cited by 1,886
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
Self-citationPhosphatidic Acid-Mediated Mitogenic Activation of mTOR Signaling
Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., & Chen, J. (2001) · Science · doi:10.1126/science.1066015 · Cited by 1,055
Majumder, P. K., Febbo, P. G., Bikoff, R., Berger, R., Xue, Q., McMahon, L. M., Manola, J., Brugarolas, J., McDonnell, T. J., Golub, T. R., et al. (2004) · Nature Medicine · doi:10.1038/nm1052 · Cited by 964
Gottlob, K., Majewski, N., Kennedy, S., Kandel, E., Robey, R. B., & Hay, N. (2001) · Genes & Development · doi:10.1101/gad.889901 · Cited by 961
Self-citationIsolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells
Sabers, C. J., Martin, M. M., Brunn, G. J., Williams, J. M., Dumont, F. J., Wiederrecht, G., & Abraham, R. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.815 · Cited by 887
Tee, A. R., Fingar, D. C., Manning, B. D., Kwiatkowski, D. J., Cantley, L. C., & Blenis, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202476899 · Cited by 827
RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.
Chiu, M. I., Katz, H., & Berlin, V (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12574 · Cited by 481
Flagged first, then by citations
Research works printed but not linked: 203
- 10.1146/annurev.immunol.14.1.483 · DOI
- 10.1038/318533a0 · DOI
- 10.1038/ng1095-115 · DOI
- 10.1016/j.ccr.2004.05.024 · DOI
- 1996, EMBO J., 15, 658, 10.1002/j.1460-2075.1996.tb00398.x · DOI
- 1996, J. Virol., 70, 8993, 10.1128/jvi.70.12.8993-8996.1996 · DOI
- 10.1073/pnas.100391597 · DOI
- 10.1074/jbc.M308573200 · DOI
- 10.1038/nrc1362 · DOI
- 10.1016/S0968-0004(00)01563-2 · DOI · Paper page
- 10.1016/S0968-0004(01)01958-2 · DOI · Paper page
- 10.1038/369756a0 · DOI · Paper page
- 10.1038/377441a0 · DOI
- 10.1128/MCB.24.7.2986-2997.2004 · DOI
- 1996, EMBO J., 15, 5256, 10.1002/j.1460-2075.1996.tb00911.x · DOI
- 10.1126/science.277.5322.99 · DOI · Paper page
- 10.1073/pnas.95.4.1432 · DOI
- 10.1128/MCB.22.13.4499-4511.2002 · DOI
- 10.1073/pnas.2336098100 · DOI
- 10.1073/pnas.96.8.4240 · DOI
- 10.1016/S0092-8674(00)81653-0 · DOI · Paper page
- 10.1007/s004390000348 · DOI
- 1994, Mol. Cell. Biol., 14, 4902
- 10.1083/jcb.200210141 · DOI
- 10.1073/pnas.92.11.4947 · DOI · Paper page
- 10.1074/jbc.C300534200 · DOI
- 10.1126/science.274.5285.239 · DOI
- 10.1074/jbc.M301142200 · DOI
- 10.1038/370071a0 · DOI
- 10.1091/mbc.E03-08-0594 · DOI
- 10.1128/MMBR.66.4.579-591.2002 · DOI
- 10.1074/jbc.M205838200 · DOI
- 10.1016/S1357-2725(98)00132-0 · DOI
- 10.1126/science.1063518 · DOI · Paper page
- 10.1101/gad.10.15.1904 · DOI
- 10.1128/MCB.23.24.8925-8933.2003 · DOI
- 10.1038/nrc969 · DOI
- 1999, Mol. Cell. Biol., 19, 4525, 10.1128/MCB.19.6.4525 · DOI
- 1985, J. Biol. Chem., 260, 5493, 10.1016/S0021-9258(18)89049-4 · DOI
- 1987, J. Biol. Chem., 262, 380, 10.1016/S0021-9258(19)75938-9 · DOI
- 10.1016/0092-8674(93)90618-Z · DOI · Paper page
- 10.1016/j.cub.2003.11.021 · DOI
- 10.1074/jbc.M307949200 · DOI
- 10.1101/gad.995802 · DOI · Paper page
- 10.1128/MCB.24.1.200-216.2004 · DOI
- 10.1080/030097400750001860 · DOI
- 1997, Cancer Res., 57, 5041
- 10.1101/gad.901101 · DOI
- 10.1038/ncb847 · DOI
- 10.1016/S1097-2765(03)00220-X · DOI · Paper page
- 10.1074/jbc.M309999200 · DOI
- 10.1101/gad.12.4.502 · DOI
- 10.1101/gad.13.11.1422 · DOI
- 10.1146/annurev.biochem.68.1.913 · DOI
- 2001, Genes & Dev., 15, 2852, 10.1101/gad.912401 · DOI · Paper page
- 10.1074/jbc.M202678200 · DOI
- 10.1016/S0092-8674(03)00975-9 · DOI
- 2002, Cancer Res., 62, 6141
- 10.1074/jbc.M207211200 · DOI
- 1995, EMBO J., 14, 5701, 10.1002/j.1460-2075.1995.tb00257.x · DOI
- 10.1042/bst0240234 · DOI
- 10.1128/MCB.23.23.8862-8877.2003 · DOI
- 10.1016/S0092-8674(02)00833-4 · DOI
- 10.1146/annurev.biochem.67.1.821 · DOI
- 10.1126/stke.2122003re15 · DOI
- 10.1016/S0014-5793(99)01094-7 · DOI
- 10.1091/mbc.5.1.105 · DOI
- 10.1016/S0960-9822(00)00567-4 · DOI
- Hershey J.W.B . and Merrick, W.C. 2000. Pathway and mechanism of initiation of protein synthesis. In Translational control of gene expression (ed. M.B. Mathews), pp. 33-88. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
- Hershey J.W.B . and Miyamoto, S. 2000. Translational control and cancer. In Translational control of gene expression (ed. M.B. Mathews), pp. 637-654. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
- 2004, Curr. Top. Microbiol. Immunol., 279, 339
- 2001, Cancer Res., 61, 3373
- 10.1038/sj.onc.1205792 · DOI
- 10.1038/ncb839 · DOI · Paper page
- 10.1016/S0092-8674(03)00929-2 · DOI · Paper page
- 10.1016/S0092-8674(01)00475-5 · DOI
- 10.1038/nrm1018 · DOI
- 10.1083/jcb.jcb.200206108 · DOI
- 10.1093/emboj/16.12.3693 · DOI · Paper page
- 10.1086/302381 · DOI
- 10.1126/science.1067020 · DOI · Paper page
- 10.1006/excr.1999.4690 · DOI
- 10.1126/science.273.5280.1402 · DOI
- 10.1074/jbc.M011068200 · DOI
- 10.1016/S0092-8674(04)00115-1 · DOI · Paper page
- 10.1016/S0968-0004(98)01340-1 · DOI
- 2001, J. Neurosci., 21, 382, 10.1523/JNEUROSCI.21-02-00382.2001 · DOI
- 10.1016/S0092-8674(02)00808-5 · DOI
- 10.1016/S1097-2765(03)00114-X · DOI
- 1992, EMBO J., 11, 4153, 10.1002/j.1460-2075.1992.tb05508.x · DOI
- 10.1016/S0896-6273(01)00508-6 · DOI
- 10.1016/0092-8674(93)90144-F · DOI
- 10.1093/hmg/11.5.525 · DOI
- 10.1038/35010550 · DOI
- 1992, Mol. Cell. Biol., 12, 1234
- 10.1038/345544a0 · DOI
- 10.1074/jbc.C200510200 · DOI
- 10.1126/science.7939721 · DOI
- 2002, Cancer Res., 62, 6475
- 10.1042/BJ20030577 · DOI
- 10.1016/S0960-9822(02)01091-6 · DOI
- 10.1074/jbc.M310872200 · DOI
- 2000, Genetics, 155, 611, 10.1093/genetics/155.2.611 · DOI
- 1995, Mol. Cell. Biol., 15, 4990, 10.1128/MCB.15.9.4990 · DOI
- 10.1016/0192-0561(94)90091-4 · DOI
- 10.1016/S1097-2765(02)00568-3 · DOI · Paper page
- 1991, J. Biol. Chem., 266, 2383, 10.1016/S0021-9258(18)52255-9 · DOI
- 10.1016/S1097-2765(01)80003-4 · DOI
- 10.1056/NEJMp038141 · DOI
- Mathews M.B ., Sonenberg, N., and Hershey, J.W.B. 2000. Origins and principles of translational control. In Translational control of gene expression (ed. M.B. Mathews), pp. 1-31. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
- 2002, Genetics, 161, 1053, 10.1093/genetics/161.3.1053 · DOI
- 10.1101/gad.285504 · DOI
- 1996, Mol. Cell. Biol., 16, 2857, 10.1128/MCB.16.6.2857 · DOI
- Meyuhas O . and Hornstein, E. 2000. Translational control of TOP mRNAs. In Translational control of gene expression (ed. M.B. Mathews), pp. 671-694. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
- 10.1038/35078571 · DOI
- 10.1128/MCB.23.24.9117-9126.2003 · DOI
- 10.4161/cbt.2.2.334 · DOI
- 10.1126/science.285.5436.2126 · DOI
- 10.1128/MCB.20.10.3558-3567.2000 · DOI
- 1999, Biochem. J., 344, 427, 10.1042/bj3440427 · DOI
- 10.1074/jbc.M204802200 · DOI
- 10.1073/pnas.171076798 · DOI
- 10.1016/S0022-2836(02)00328-5 · DOI
- 10.1074/jbc.C200665200 · DOI
- 10.1101/gad.845700 · DOI
- 10.1111/j.1356-9597.2004.00727.x · DOI
- 10.1242/jcs.00661 · DOI
- 10.1038/371762a0 · DOI
- 10.1038/35050135 · DOI
- 10.1128/MCB.24.8.3112-3124.2004 · DOI
- 10.1101/gad.1089403 · DOI
- 10.1073/pnas.96.8.4438 · DOI
- 10.1074/jbc.275.10.7416 · DOI
- 10.1073/pnas.171060098 · DOI
- 1996, Mol. Cell. Biol., 16, 6573, 10.1128/MCB.16.11.6573 · DOI
- 10.1016/S0092-8674(01)00333-6 · DOI
- 10.1038/ncb840 · DOI · Paper page
- 10.1074/jbc.273.22.14002 · DOI
- 10.1091/mbc.10.4.987 · DOI
- 10.1093/emboj/18.1.270 · DOI
- 10.1074/jbc.M308781200 · DOI
- 10.1038/ncb763 · DOI
- 10.1016/S1097-2765(03)00395-2 · DOI · Paper page
- 10.1128/MCB.23.20.7315-7328.2003 · DOI · Paper page
- 10.1093/emboj/19.3.434 · DOI
- Raught B ., Gingras, A.-C., and Sonenberg, N. 2000b. Regulation of ribosomal recruitment in eukaryotes. In Translational control of gene expression (ed. M.B. Mathews), pp. 245-294. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
- 10.1038/sj.emboj.7600193 · DOI
- 10.1074/jbc.M201142200 · DOI
- 10.1016/S0079-6603(02)72073-4 · DOI
- 10.1038/nrc1015 · DOI
- 10.1038/nm1042 · DOI
- 10.1016/0092-8674(94)90570-3 · DOI · Paper page
- 10.1016/j.cub.2003.12.005 · DOI
- 10.1038/ncb996 · DOI
- 10.1016/S1535-6108(03)00275-7 · DOI
- 10.1038/sj.onc.1203739 · DOI
- 10.1016/S0960-9822(02)00762-5 · DOI
- 10.1016/S0960-9822(03)00329-4 · DOI
- 10.1038/35096067 · DOI
- 10.1016/S0092-8674(00)00117-3 · DOI
- 10.1073/pnas.93.24.13780 · DOI
- 1999, Mol. Cell. Biol., 19, 2485, 10.1128/MCB.19.4.2485 · DOI
- 10.1073/pnas.95.13.7772 · DOI
- 2000, Cancer Res., 60, 3504
- 1994, Cancer Res., 54, 2313
- 10.1074/jbc.273.29.18528 · DOI
- 1995, Cancer Res., 55, 1982
- 10.1093/emboj/17.22.6649 · DOI
- 10.1016/S0092-8674(03)01021-3 · DOI
- 10.1006/excr.2000.5130 · DOI
- 1993, Gene Expr., 3, 317
- 10.1038/ncb995 · DOI
- 10.1128/MCB.22.23.8101-8113.2002 · DOI
- 10.1074/jbc.M306553200 · DOI
- 10.1046/j.1365-2443.2000.00365.x · DOI
- 10.1074/jbc.M103237200 · DOI
- 10.1038/sj.onc.1203446 · DOI
- 10.1128/MCB.21.24.8671-8683.2001 · DOI
- 10.1073/pnas.012605299 · DOI · Paper page
- 10.1016/S0092-8674(01)00332-4 · DOI
- 10.1074/jbc.M303257200 · DOI
- 10.1016/S0960-9822(03)00506-2 · DOI · Paper page
- 2003, Cancer Res., 63, 364
- 10.1038/35010581 · DOI
- 10.1038/nm1001-1128 · DOI
- 1989, J. Biol. Chem., 264, 2773, 10.1016/S0021-9258(19)81680-0 · DOI
- 10.1128/MCB.20.21.8035-8046.2000 · DOI · Paper page
- 10.1126/science.277.5327.805 · DOI · Paper page
- 10.1074/jbc.M313874200 · DOI
- 10.1038/70293 · DOI
- 10.1038/nrc839 · DOI
- 10.1073/pnas.93.9.4076 · DOI
- 10.1093/emboj/16.8.1909 · DOI
- 10.1038/nature02369 · DOI
- 10.1074/jbc.270.27.16409 · DOI
- 10.1074/jbc.C000482200 · DOI
- 10.1074/jbc.272.10.6097 · DOI
- 1994, J. Biol. Chem., 269, 16333, 10.1016/S0021-9258(17)34012-7 · DOI
- 10.1046/j.1471-4159.1998.70020572.x · DOI
- 1998, Mol. Cell. Biol., 18, 4463, 10.1128/MCB.18.8.4463 · DOI
200 of 203 shown
Cited by
Sorted by citations
Items 101–176 of 176
Kim, J.-H., Kim, J. E., Liu, H.-Y., Cao, W., & Chen, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708568200 · Cited by 154
Coordinate Autophagy and mTOR Pathway Inhibition Enhances Cell Death in Melanoma
Xie, X., White, E. P., & Mehnert, J. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055096 · Cited by 150
Thomson, D. M., Fick, C. A., & Gordon, S. E. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00915.2007 · Cited by 153
Metformin Targets Multiple Signaling Pathways in Cancer
Lei, Y., Yi, Y., Liu, Y., Liu, X., Keller, E. T., Qian, C.-N., Zhang, J., & Lu, Y. (2017) · Chinese Journal of Cancer · doi:10.1186/s40880-017-0184-9 · Cited by 152
Mechanisms of vitamin D action in skeletal muscle
Montenegro, K. R., Cruzat, V., Carlessi, R., & Newsholme, P. (2019) · Nutrition Research Reviews · doi:10.1017/s0954422419000064 · Cited by 147
Defective autophagy in atherosclerosis: to die or to senesce?
Grootaert, M. O. J., Roth, L., Schrijvers, D. M., De Meyer, G. R. Y., & Martinet, W. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7687083 · Cited by 147
De Gregorio, D., Popic, J., Enns, J. P., Inserra, A., Skalecka, A., Markopoulos, A., Posa, L., Lopez-Canul, M., He, Q., Lafferty, C. K., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020705118 · Cited by 139
Self-citationPanja, D., Kenney, J. W., D’Andrea, L., Zalfa, F., Vedeler, A., Wibrand, K., Fukunaga, R., Bagni, C., Proud, C. G., & Bramham, C. R. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.016 · Cited by 143
Activation of AMPK under Hypoxia: Many Roads Leading to Rome
Dengler, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072428 · Cited by 133
PP2A regulatory subunit PP2A-B' counteracts S6K phosphorylation
Hahn, K., Miranda, M., Francis, V. A., Vendrell, J., Zorzano, A., & Teleman, A. A. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.03.015 · Cited by 131
Mtor is necessary for proper satellite cell activity and skeletal muscle regeneration
Zhang, P., Liang, X., Shan, T., Jiang, Q., Deng, C., Zheng, R., & Kuang, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.05.032 · Cited by 133
Ageing and the regulation of protein synthesis: a balancing act?
Tavernarakis, N. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.02.004 · Cited by 129
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
Hirota, Y., Cha, J., Yoshie, M., Daikoku, T., & Dey, S. K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108180108 · Cited by 125
mTOR complex 1: a key player in neuroadaptations induced by drugs of abuse
Neasta, J., Barak, S., Hamida, S. B., & Ron, D. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12725 · Cited by 114
ESFAHANIAN, N., SHAKIBA, Y., NIKBIN, B., SORAYA, H., MALEKI-DIZAJI, N., GHAZI-KHANSARI, M., & GARJANI, A. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2012.753 · Cited by 120
Fortin, D. A., Srivastava, T., Dwarakanath, D., Pierre, P., Nygaard, S., Derkach, V. A., & Soderling, T. R. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6034-11.2012 · Cited by 120
A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation regulates autophagy
Hu, G., McQuiston, T., Bernard, A., Park, Y.-D., Qiu, J., Vural, A., Zhang, N., Waterman, S. R., Blewett, N. H., Myers, T. G., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3189 · Cited by 116
Rapamycin reverses status epilepticus-induced memory deficits and dendritic damage
Brewster, A. L., Lugo, J. N., Patil, V. V., Lee, W. L., Qian, Y., Vanegas, F., & Anderson, A. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057808 · Cited by 112
Decreased mTOR signaling pathway in human idiopathic autism and in rats exposed to valproic acid
Nicolini, C., Ahn, Y., Michalski, B., Rho, J. M., & Fahnestock, M. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0184-4 · Cited by 109
Rheb and Rags come together at the lysosome to activate mTORC1
Groenewoud, M. J., & Zwartkruis, F. J. T. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130037 · Cited by 96
Caveolin-1 and Accelerated Host Aging in the Breast Tumor Microenvironment
Mercier, I., Camacho, J., Titchen, K., Gonzales, D. M., Quann, K., Bryant, K. G., Molchansky, A., Milliman, J. N., Whitaker-Menezes, D., Sotgia, F., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.03.017 · Cited by 96
Met acts on Mdm2 via mTOR to signal cell survival during development
Moumen, A., Patané, S., Porras, A., Dono, R., & Maina, F. (2007) · Development · doi:10.1242/dev.02820 · Cited by 95
mTOR signaling and Alzheimer's disease: What we know and where we are?
Davoody, S., Asgari Taei, A., Khodabakhsh, P., & Dargahi, L. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14463 · Cited by 96
Nrf2 Transcription Factor Can Directly Regulate mTOR
Bendavit, G., Aboulkassim, T., Hilmi, K., Shah, S., & Batist, G. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.760249 · Cited by 95
Hamilton, T. L., Stoneley, M., Spriggs, K. A., & Bushell, M. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340012 · Cited by 91
Kim, J.-H., Yoon, M.-S., & Chen, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051516 · Cited by 92
Altering chemosensitivity by modulating translation elongation
Robert, F., Carrier, M., Rawe, S., Chen, S., Lowe, S., & Pelletier, J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005428 · Cited by 90
Metformin for treatment of fragile X syndrome and other neurological disorders
Gantois, I., Popic, J., Khoutorsky, A., & Sonenberg, N. (2019) · Annual Review of Medicine · doi:10.1146/annurev-med-081117-041238 · Cited by 87
Self-citationNutrition and longevity—From mechanisms to uncertainties
Ekmekcioglu, C. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2019.1676698 · Cited by 87
mTOR-Dependent Cell Proliferation in the Brain
Ryskalin, L., Lazzeri, G., Flaibani, M., Biagioni, F., Gambardella, S., Frati, A., & Fornai, F. (2017) · BioMed Research International · doi:10.1155/2017/7082696 · Cited by 86
Aguilar-Valles, A., Haji, N., De Gregorio, D., Matta-Camacho, E., Eslamizade, M. J., Popic, J., Sharma, V., Cao, R., Rummel, C., Tanti, A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04883-5 · Cited by 82
Self-citationShi, X., Miller, J. S., Harper, L. J., Poole, R. L., Gould, T. J., & Unterwald, E. M. (2014) · Psychopharmacology · doi:10.1007/s00213-014-3491-8 · Cited by 79
Increased mTOR activation in idiopathic multicentric Castleman disease
Arenas, D. J., Floess, K., Kobrin, D., Pai, R.-A. L., Srkalovic, M. B., Tamakloe, M.-A., Rasheed, R., Ziglar, J., Khor, J., Parente, S. A. T., et al. (2020) · Blood · doi:10.1182/blood.2019002792 · Cited by 83
TCR-Dependent Translational Control of GATA-3 Enhances Th2 Differentiation
Cook, K. D., & Miller, J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902544 · Cited by 79
From molecules to neural morphology: understanding neuroinflammation in autism spectrum condition
Young, A. M. H., Chakrabarti, B., Roberts, D., Lai, M.-C., Suckling, J., & Baron-Cohen, S. (2016) · Molecular Autism · doi:10.1186/s13229-016-0068-x · Cited by 76
Rosario, F. J., Gupta, M. B., Myatt, L., Powell, T. L., Glenn, J. P., Cox, L., & Jansson, T. (2019) · Scientific Reports · doi:10.1038/s41598-018-36265-8 · Cited by 77
Tremblay, F., Jacques, H., & Marette, A. (2005) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/01.mco.0000172589.55434.03 · Cited by 71
Matheson, H., Veerbeek, J. H. W., Charnock‐Jones, D. S., Burton, G. J., & Yung, H. W. (2016) · The Journal of Physiology · doi:10.1113/jp271073 · Cited by 71
MCRS1 Binds and Couples Rheb to Amino Acid-Dependent mTORC1 Activation
Fawal, M.-A., Brandt, M., & Djouder, N. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.02.010 · Cited by 70
Sha, L.-Z., Xing, X.-L., Zhang, D., Yao, Y., Dou, W.-C., Jin, L.-R., Wu, L.-W., & Xu, Q. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039152 · Cited by 70
Du, C., Zhang, T., Xiao, X., Shi, Y., Duan, H., & Ren, Y. (2017) · Biochemical Journal · doi:10.1042/bcj20170272 · Cited by 68
PLD regulates myoblast differentiation through the mTOR-IGF2 pathway
Yoon, M.-S., & Chen, J. (2008) · Journal of Cell Science · doi:10.1242/jcs.022566 · Cited by 67
Normand, E. A., Crandall, S. R., Thorn, C. A., Murphy, E. M., Voelcker, B., Browning, C., Machan, J. T., Moore, C. I., Connors, B. W., & Zervas, M. (2013) · Neuron · doi:10.1016/j.neuron.2013.03.030 · Cited by 67
Zinc, future mono/adjunctive therapy for depression: Mechanisms of antidepressant action
Nowak, G. (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2015.01.015 · Cited by 65
Rapamycin attenuates the expression of cocaine‐induced place preference and behavioral sensitization
Bailey, J., Ma, D., & Szumlinski, K. K. (2012) · Addiction Biology · doi:10.1111/j.1369-1600.2010.00311.x · Cited by 61
Amino acid starvation has opposite effects on mitochondrial and cytosolic protein synthesis
Johnson, M. A., Vidoni, S., Durigon, R., Pearce, S. F., Rorbach, J., He, J., Brea-Calvo, G., Minczuk, M., Reyes, A., Holt, I. J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093597 · Cited by 63
Mitochondrial stress-dependent regulation of cellular protein synthesis
Topf, U., Uszczynska-Ratajczak, B., & Chacinska, A. (2019) · Journal of Cell Science · doi:10.1242/jcs.226258 · Cited by 52
Jackson, J. B., & Pallas, D. C. (2012) · Neoplasia · doi:10.1593/neo.12768 · Cited by 60
Aberrant AKT activation drives well-differentiated liposarcoma
Gutierrez, A., Snyder, E. L., Marino-Enriquez, A., Zhang, Y.-X., Sioletic, S., Kozakewich, E., Grebliunaite, R., Ou, W.-B., Sicinska, E., Raut, C. P., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106127108 · Cited by 58
Ma, Y., Zhu, M. J., Uthlaut, A. B., Nijland, M. J., Nathanielsz, P. W., Hess, B. W., & Ford, S. P. (2011) · Placenta · doi:10.1016/j.placenta.2011.01.007 · Cited by 58
“However, mTOR, as a nutrient sensor that also promote cell growth via regulating protein synthesis, and its upstream signal, the insulinAkt signaling, were not altered by maternal undernutrition in the current study [19,45].”
Chauvin, C., Salhi, S., & Jean-Jean, O. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00035-07 · Cited by 58
Lee, H.-K., Kwon, B., Lemere, C. A., de la Monte, S., Itamura, K., Ha, A. Y., & Querfurth, H. W. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161029 · Cited by 57
Insulin-Like Growth Factor Signaling as a Therapeutic Target in Pancreatic Cancer
Rieder, S., W. Michalski, C., Friess, H., & Kleeff, >. (2011) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152011795677454 · Cited by 50
Mitochondrial turnover and homeostasis in ageing and neurodegeneration
Markaki, M., & Tavernarakis, N. (2020) · FEBS Letters · doi:10.1002/1873-3468.13802 · Cited by 50
Sudhan, D. R., Guerrero-Zotano, A., Won, H., González Ericsson, P., Servetto, A., Huerta-Rosario, M., Ye, D., Lee, K.-M., Formisano, L., Guo, Y., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2019.12.013 · Cited by 49
Rantamäki, T., & Kohtala, S. (2020) · Pharmacological Reviews · doi:10.1124/pr.119.018697 · Cited by 45
Energy metabolism and rheumatic diseases: from cell to organism
Spies, C. M., Straub, R. H., & Buttgereit, F. (2012) · Arthritis Research & Therapy · doi:10.1186/ar3885 · Cited by 47
Verheijden, S., Beckers, L., Casazza, A., Butovsky, O., Mazzone, M., & Baes, M. (2015) · Glia · doi:10.1002/glia.22831 · Cited by 40
Coupling between Nutrient Availability and Thyroid Hormone Activation
Lartey, L. J., Werneck-de-Castro, J. P., O-Sullivan, I., Unterman, T. G., & Bianco, A. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.665505 · Cited by 41
Metabolic control of antifungal drug resistance
Robbins, N., Collins, C., Morhayim, J., & Cowen, L. E. (2010) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2009.07.004 · Cited by 40
Qin, T., Barron, L., Xia, L., Huang, H., Villarreal, M. M., Zwaagstra, J., Collins, C., Yang, J., Zwieb, C., Kodali, R., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.13343 · Cited by 40
Licorice flavonoid oil enhances muscle mass in KK-A mice
Yoshioka, Y., Yamashita, Y., Kishida, H., Nakagawa, K., & Ashida, H. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.05.024 · Cited by 39
Niere, F., Namjoshi, S., Song, E., Dilly, G. A., Schoenhard, G., Zemelman, B. V., Mechref, Y., & Raab-Graham, K. F. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.055079 · Cited by 38
Jiang, S.-L., Guan, Y.-D., Chen, X.-S., Ge, P., Wang, X.-L., Lao, Y.-Z., Xiao, S.-S., Zhang, Y., Yang, J.-M., Xu, X.-J., et al. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-018-0165-9 · Cited by 37
Djuzenova, C. S., Fiedler, V., Memmel, S., Katzer, A., Hartmann, S., Krohne, G., Zimmermann, H., Scholz, C.-J., Polat, B., Flentje, M., et al. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.08.013 · Cited by 34
Bi, C., Zhang, X., Lu, T., Zhang, X., Wang, X., Meng, B., Zhang, H., Wang, P., Vose, J. M., Chan, W. C., et al. (2017) · Haematologica · doi:10.3324/haematol.2016.159160 · Cited by 32
Wei, Y., Reveal, B., Cai, W., & Lilly, M. A. (2016) · G3 Genes|Genomes|Genetics · doi:10.1534/g3.116.035337 · Cited by 31
Kroczynska, B., Rafidi, R. L., Majchrzak-Kita, B., Kosciuczuk, E. M., Blyth, G. T., Jemielity, J., Warminska, Z., Saleiro, D., Mehrotra, S., Arslan, A. D., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664995 · Cited by 29
Transcription factors and cognate signalling cascades in the regulation of autophagy
Chandra, V., Bhagyaraj, E., Parkesh, R., & Gupta, P. (2016) · Biological Reviews · doi:10.1111/brv.12177 · Cited by 26
Wu, X., Yu, J., Yan, J., Dai, J., Si, L., Chi, Z., Sheng, X., Cui, C., Ma, M., Tang, H., et al. (2018) · Cancer Biology & Therapy · doi:10.1080/15384047.2018.1435221 · Cited by 25
Autophagy: a killer or guardian of vascular smooth muscle cells
Zhang, Y.-Y., Shi, Y.-N., Zhu, N., Wang, W., Deng, C.-F., Xie, X.-J., Liao, D.-F., & Qin, L. (2020) · Journal of Drug Targeting · doi:10.1080/1061186x.2019.1705312 · Cited by 24
Efficient genetic editing of human intestinal organoids using ribonucleoprotein-based CRISPR
Skoufou-Papoutsaki, N., Adler, S., D'Santos, P., Mannion, L., Mehmed, S., Kemp, R., Smith, A., Perrone, F., Nayak, K., Russell, A., et al. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.050279 · Cited by 22
“This pathway is an important regulator of cell proliferation and metabolism (Hay and Sonenberg, 2004; Guertin and Sabatini, 2007). mTORC1 is also known to be important for controlling cell size, with activated mTORC1 leading to larger cells (Fingar et al., 2002).”
Zhang, L., Wang, X., Wu, Y., Lu, X., Chidiac, P., Wang, G., & Feng, Q. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13500 · Cited by 17
Genes related to heat tolerance in cattle—a review
Zeng, L., Qu, K., Zhang, J., Huang, B., & Lei, C. (2023) · Animal Biotechnology · doi:10.1080/10495398.2022.2047995 · Cited by 13
Chwin, N., & Kiryk, A. (2024) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2024-2657 · Cited by 3
Metadata
- Authors
- Hay, N., & Sonenberg, N.
- Affiliations
- University of Illinois Chicago (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-08-15
- Volume
- 18
- Issue
- 16
- Pages
- 1926-1945
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2129585918
- Cited by
- 4,181
- References
- 13
- Citations by year
- 2026: 40 · 2025: 75 · 2024: 94 · 2023: 144 · 2022: 145 · 2021: 188 · 2020: 208 · 2019: 184 · 2018: 216 · 2017: 219 · 2016: 249 · 2015: 265 · 2014: 280 · 2013: 274 · 2012: 284
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@McGill (McGill) (submittedVersion, cc-by-nc)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- Canadian Institutes of Health Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- mTOR, TOR signaling, protein synthesis regulation, cell growth, cell proliferation, downstream targets, phosphorylation, cancer, synaptic plasticity
- MeSH terms
- Animals, Cell Division, Energy Metabolism, Growth Substances, Neoplasms, Peptide Initiation Factors, Phosphorylation, Protein Kinases, Transcription, Genetic, Protein Biosynthesis, Ribosomal Protein S6 Kinases, TOR Serine-Threonine Kinases
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review