Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway

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 · see citing works

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104 · see citing works

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha.

Alessi, D., James, S., Downes, C., Holmes, A. B., Gaffney, P., Reese, C., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 3,047 · see citing works

Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction

Burgering, B. M. T., & Coffer, P. J. (1995) · Nature · doi:10.1038/376599a0 · Cited by 2,113 · see citing works

New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway

Cantley, L. C., & Neel, B. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4240 · Cited by 2,007 · see citing works

The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase

Franke, T. F., Yang, S., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., & Tsichlis, P. N. (1995) · Cell · doi:10.1016/0092-8674(95)90534-0 · Cited by 2,006 · see citing works

The PI3K‒PDK1 connection: more than just a road to PKB

Vanhaesebroeck, B., & Alessi, D. R. (2000) · Biochemical Journal · doi:10.1042/bj3460561 · Cited by 1,632 · see citing works

Direct Regulation of the Akt Proto-Oncogene Product by Phosphatidylinositol-3,4-bisphosphate

Franke, T. F., Kaplan, D., Cantley, L., & Toker, A. (1997) · Science · doi:10.1126/science.275.5300.665 · Cited by 1,609 · see citing works

Amino Acid Sufficiency and mTOR Regulate p70 S6 Kinase and eIF-4E BP1 through a Common Effector Mechanism

Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14484 · Cited by 1,370 · see citing works

Cellular Function of Phosphoinositide 3-Kinases: Implications for Development, Immunity, Homeostasis, and Cancer

Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J. F., & Waterfield, M. D. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.615 · Cited by 1,204 · see citing works

Dual Role of Phosphatidylinositol-3,4,5-trisphosphate in the Activation of Protein Kinase B

Stokoe, D., Stephens, L. R., Copeland, T., Gaffney, P. R. J., Reese, C. B., Painter, G. F., Holmes, A. B., McCormick, F. P., & Hawkins, P. T. (1997) · Science · doi:10.1126/science.277.5325.567 · Cited by 1,202 · see citing works

Ten years of protein kinase B signalling: a hard Akt to follow

Brazil, D. P., & Hemmings, B. A. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01958-2 · Cited by 1,177 · see citing works

The lipid phosphatase activity of PTEN is critical for its tumor supressor function

Myers, M. P., Pass, I., Batty, I. H., KAAY, J. V. D., Stolarov, J. P., Hemmings, B. A., Wigler, M. H., Downes, C. P., & Tonks, N. K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13513 · Cited by 1,161 · see citing works

Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases

Chung, J., Kuo, C. J., Crabtree, G. R., & Blenis, J. (1992) · Cell · doi:10.1016/0092-8674(92)90643-q · Cited by 1,151 · see citing works

Phosphatidic 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 · see citing works

Mutational Analysis in a Cohort of 224 Tuberous Sclerosis Patients Indicates Increased Severity of TSC2, Compared with TSC1, Disease in Multiple Organs

Dabora, S. L., Jóźwiak, S., Franz, D. N., Roberts, P. S., Nieto, A., Chung, J., Choy, Y.-S., Reeve, M. P., Thiele, E. A., Egelhoff, J. C., et al. (2001) · The American Journal of Human Genetics · doi:10.1086/316951 · Cited by 998 · see citing works

The Role of Phosphoinositide 3-Kinase Lipid Products in Cell Function

Rameh, L. E., & Cantley, L. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8347 · Cited by 990 · see citing works

Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR

Neshat, M. S., Mellinghoff, I. K., Tran, C., Stiles, B. L., THOMAS, G. V., Petersen, R., Frost, P., Gibbons, J. J., Wu, H., & Sawyers, C. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171076798 · Cited by 968 · see citing works

Mammalian TOR: a homeostatic ATP sensor

Dennis, P. B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S. C., & Thomas, G. (2001) · Science · doi:10.1126/science.1063518 · Cited by 962 · see citing works

Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation

NAVÉ, B. T., Ouwens, D. M., Withers, D. J., Alessi, D. R., & Shepherd, P. R. (1999) · Biochemical Journal · doi:10.1042/bj3440427 · Cited by 926 · see citing works

Phosphorylation and Activation of p70 ^s6k by PDK1

Pullen, N., Dennis, P. B., Andjelkovic, M., Dufner, A., Kozma, S. C., Hemmings, B. A., & Thomas, G. (1998) · Science · doi:10.1126/science.279.5351.707 · Cited by 826 · see citing works

PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway

Sun, H., Lesche, R., Li, D., Liliental, J., Zhang, H., Gao, J., Gavrilova, N. J., Mueller, B., Liu, X., & Wu, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6199 · Cited by 796 · see citing works

PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase

Chung, J., Grammar, T. C., Lemon, K. P., Kazlauskas, A., & Blenis, J. (1994) · Nature · doi:10.1038/370071a0 · Cited by 719 · see citing works

A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells.

Sekulić, A., Hudson, C. C., Homme, J. L., Yin, P., Otterness, D. M., Karnitz, L. M., & Abraham, R. T. (2000) · PubMed · Cited by 708 · see citing works

Frequent inactivation of PTEN/MMAC1 in primary prostate cancer.

Cairns, P., Okami, K., Halachmi, S., Halachmi, N., Esteller, M., Herman, J. G., Jen, J., Isaacs, W. B., Bova, G. S., & Sidransky, D. (1997) · PubMed · Cited by 707 · see citing works

A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells

Kwiatkowski, D. J. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.5.525 · Cited by 663 · see citing works

Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression

Whang, Y. E., Wu, X., Suzuki, H., Reiter, R. E., Tran, C., Vessella, R. L., SAID, J. W., Isaacs, W. B., & Sawyers, C. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5246 · Cited by 639 · see citing works

Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase‐1 and p70 S6 kinase

Alessi, D. R., Barry Caudwell, F., Andjelkovic, M., Hemmings, B. A., & Cohen, P. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01370-1 · Cited by 628 · see citing works

Serum and glucocorticoid‐inducible kinase (SGK) is a target of the PI 3‐kinase‐stimulated signaling pathway

Park, J., Leong, M., Buse, P., Maiyar, A. C., Firestone, G. L., & Hemmings, B. (1999) · EMBO Journal · doi:10.1093/emboj/18.11.3024 · Cited by 588 · see citing works

Regulation of G 1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway

Ramaswamy, S., Nakamura, N., Vázquez, F., Batt, D. B., Perera, S., Roberts, T. M., & Sellers, W. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2110 · Cited by 575 · see citing works

Determination of the Specific Substrate Sequence Motifs of Protein Kinase C Isozymes

Nishikawa, K., Toker, A., Johannes, F., Songyang, Z., & Cantley, L. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.952 · Cited by 557 · see citing works

The Drosophila Tuberous Sclerosis Complex Gene Homologs Restrict Cell Growth and Cell Proliferation

Tapon, N., Ito, N., Dickson, B. J., Treisman, J. E., & Hariharan, I. K. (2001) · Cell · doi:10.1016/s0092-8674(01)00332-4 · Cited by 542 · see citing works

Drosophila Tsc1 Functions with Tsc2 to Antagonize Insulin Signaling in Regulating Cell Growth, Cell Proliferation, and Organ Size

Potter, C. J., Huang, H., & Xu, T. (2001) · Cell · doi:10.1016/s0092-8674(01)00333-6 · Cited by 522 · see citing works

A motif-based profile scanning approach for genome-wide prediction of signaling pathways

Yaffe, M. B., Leparc, G. G., Lai, J., Obata, T., Volinia, S., & Cantley, L. C. (2001) · Nature Biotechnology · doi:10.1038/86737 · Cited by 517 · see citing works

TSC1 and TSC2 tumor suppressors antagonize insulin signaling in cell growth.Preprint

Gao, X., & Pan, D. (2001) · Genes & Development · doi:10.1101/gad.901101 · Cited by 484 · see citing works

Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway

Scott, P., Brunn, G. J., Kohn, A. D., Roth, R. A., & Lawrence, J. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7772 · Cited by 476 · see citing works

Peptide and Protein Library Screening Defines Optimal Substrate Motifs for AKT/PKB

Obata, T., Yaffe, M. B., Leparc, G., Piro, E. T., Maegawa, H., Kashiwagi, A., Kikkawa, R., & Cantley, L. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005497200 · Cited by 388 · see citing works

Regulation of the p70 S6 Kinase by Phosphorylation in Vivo

Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., Zhang, A., Comb, M. J., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16621 · Cited by 375 · see citing works

Essential Role for Protein Kinase B (PKB) in Insulin-induced Glycogen Synthase Kinase 3 Inactivation

van Weeren, P. C., de Bruyn, K. M. T., de Vries-Smits, A. M. M., Lint, J. V., & Burgering, B. M. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13150 · Cited by 365 · see citing works

Protein kinases as mediators of phosphoinositide 3-kinase signaling.

Toker, A. (2000) · Molecular Pharmacology · doi:10.1124/mol.57.4.652 · Cited by 359 · see citing works

Identification of Tuberin, the Tuberous Sclerosis-2 Product. TUBERIN POSSESSES SPECIFIC Rap1GAP ACTIVITY

Wienecke, R., König, A., & DeClue, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.16409 · Cited by 357 · see citing works

The Tuberous Sclerosis 2 Gene Product, Tuberin, Functions as a Rab5 GTPase Activating Protein (GAP) in Modulating Endocytosis

Xiao, G., Shoarinejad, F., Jin, F., Golemis, E. A., & Yeung, R. S. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6097 · Cited by 348 · see citing works

Construction and Characterization of a Conditionally Active Version of the Serine/Threonine Kinase Akt*

Kohn, A. D., Barthel, A., Kovacina, K., Boge, A., Wallach, B., Summers, S., Birnbaum, M., Scott, P. H., Lawrence, J., & Roth, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11937 · Cited by 340 · see citing works

A role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt

Aoki, M., Blazek, E., & Vogt, P. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.136 · Cited by 306 · see citing works

The 70 kDa S6 Kinase Complexes with and Is Activated by the Rho Family G Proteins Cdc42 and Rac1

Chou, M. M., & Blenis, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81257-x · Cited by 292 · see citing works

Multiple Independent Inputs Are Required for Activation of the p70 S6 Kinase

Weng, Q.-P., Andrabi, K. I., Kozlowski, M. T., Grove, J. R., & Avruch, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.5.2333 · Cited by 225 · see citing works

Coordinate regulation of translation by the PI 3-kinase and mTOR pathways

Martin, K. A., & Blenis, J. (2002) · Advances in cancer research · doi:10.1016/s0065-230x(02)86001-8 · Cited by 198 · see citing works

dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires dPDK1

Radimerski, T., Montagne, J., Rintelen, F., Stocker, H., KAAY, J. V. D., Downes, C. P., Hafen, E., & Thomas, G. (2002) · Nature Cell Biology · doi:10.1038/ncb763 · Cited by 190 · see citing works

p70 S6 Kinase Is Regulated by Protein Kinase Cζ and Participates in a Phosphoinositide 3-Kinase-Regulated Signalling Complex

Romanelli, A., Martin, K. A., Toker, A., & Blenis, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2921 · Cited by 180 · see citing works

Characterization of the Cytosolic Tuberin-Hamartin Complex

Nellist, M. D., van Slegtenhorst, M. A., Goedbloed, M., van den Ouweland, A. M. W., Halley, D. J. J., & van der Sluijs, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35647 · Cited by 176 · see citing works

Tuberous Sclerosis Complex

(1999) · doi:10.1093/oso/9780195122107.001.0001 · Cited by 175 · see citing works

Multiple keratins of cultured human epidermal cells are translated from different mRNA molecules

Fuchs, E. V., & Green, H. (1979) · Cell · doi:10.1016/0092-8674(79)90265-4 · Cited by 173 · see citing works

Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver.

Flotow, H., & Thomas, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50696-2 · Cited by 158 · see citing works

PI 3-kinase, mTOR, protein synthesis and cancer

Vogt, P. K. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02161-x · Cited by 120 · see citing works

The Use of Peptide Library for the Determination of Kinase Peptide Substrates

Songyang, Z., & Cantley, L. C. (2003) · Humana Press eBooks · doi:10.1385/0-89603-392-9:87 · Cited by 48 · see citing works

PI 3-kinase

Vermeren, S., & Welch, H. C. E. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00522-2 · Cited by 33 · see citing works

[12] Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries

Yaffe, M. B., & Cantley, L. C. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)28397-3 · Cited by 31 · see citing works

mTOR Signaling in Growth, Metabolism, and Disease

Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555 · see citing works

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 · see citing works

TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival

Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914 · see citing works

mTOR: from growth signal integration to cancer, diabetes and ageing

Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941 · see citing works

mTOR at the nexus of nutrition, growth, ageing and disease

Liu, G. Y., & Sabatini, D. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0199-y · Cited by 2,737 · see citing works

Molecular mechanisms of mTOR-mediated translational control

Ma, X. M., & Blenis, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2672 · Cited by 2,558 · see citing works

Targeting PI3K signalling in cancer: opportunities, challenges and limitations

Engelman, J. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2664 · Cited by 2,445 · see citing works

MTOR: a pharmacologic target for autophagy regulation

Kim, Y. C., & Guan, K.-L. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73939 · Cited by 2,126 · see citing works

mTOR regulation of autophagy

Jung, C. H., Ro, S.-H., Cao, J., Otto, N. M., & Kim, D.-H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.017 · Cited by 2,090 · see citing works

Activation of a metabolic gene regulatory network downstream of mTOR complex 1

Düvel, K., Yecies, J. L., Menon, S., Raman, P., Lipovsky, A. I., Souza, A. L., Triantafellow, E., Ma, Q., Gorski, R., Cleaver, S., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.022 · Cited by 2,020 · see citing works

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 · see citing works

The Tuberous Sclerosis Complex

Crino, P. B., Nathanson, K. L., & Henske, E. P. (2006) · New England Journal of Medicine · doi:10.1056/nejmra055323 · Cited by 1,793 · see citing works

Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex

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 · see citing works

Regulation of TORC1 by Rag GTPases in nutrient response

Kim, E., Goraksha-Hicks, P., Li, L., Neufeld, T. P., & Guan, K.-L. (2008) · Nature Cell Biology · doi:10.1038/ncb1753 · Cited by 1,349 · see citing works

mTOR and cancer: insights into a complex relationship

Sabatini, D. M. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1974 · Cited by 1,322 · see citing works

Phosphorylation and Functional Inactivation of TSC2 by Erk

Ma, L., Chen, Z., Erdjument-Bromage, H., Tempst, P., & Pandolfi, P. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.031 · Cited by 1,268 · see citing works

PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase

Sancak, Y., Thoreen, C. C., Peterson, T. R., Lindquist, R. A., Kang, S. A., Spooner, E., Carr, S. A., & Sabatini, D. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.003 · Cited by 1,236 · see citing works

The TSC1–TSC2 complex: a molecular switchboard controlling cell growth

Huang, J., & Manning, B. D. (2008) · Biochemical Journal · doi:10.1042/bj20080281 · Cited by 1,237 · see citing works

Insulin Activation of Rheb, a Mediator of mTOR/S6K/4E-BP Signaling, Is Inhibited by TSC1 and 2

Garami, A., Zwartkruis, F. J. T., Nobukuni, T., Joaquin, M., Roccio, M., Stocker, H., Kozma, S. C., Hafen, E., Bos, J. L., & Thomas, G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00220-x · Cited by 1,043 · see citing works

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 · see citing works

Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks

Magnuson, B., Ekim, B., & Fingar, D. C. (2012) · Biochemical Journal · doi:10.1042/bj20110892 · Cited by 1,015 · see citing works

mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways

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 · see citing works

Mutant PIK3CA promotes cell growth and invasion of human cancer cells.

Samuels, Y., Diaz, L. A., Schmidt-Kittler, O., Cummins, J. M., DeLong, L., Cheong, I., Rago, C., Huso, D. L., Lengauer, C., Kinzler, K. W., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.05.014 · Cited by 915 · see citing works

Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling

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 · see citing works

The TSC-mTOR Signaling Pathway Regulates the Innate Inflammatory Response

Weichhart, T., Costantino, G., Poglitsch, M., Rosner, M., Zeyda, M., Stuhlmeier, K. M., Kolbe, T., Stulnig, T. M., Hörl, W. H., Hengstschläger, M., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.08.012 · Cited by 801 · see citing works

The two TORCs and Akt

Bhaskar, P. T., & Hay, N. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.020 · Cited by 798 · see citing works

Regulation of mTORC1 by amino acids

Bar-Peled, L., & Sabatini, D. M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.03.003 · Cited by 773 · see citing works

RAS Interaction with PI3K: More Than Just Another Effector Pathway

Castellano, E., & Downward, J. (2011) · Genes & Cancer · doi:10.1177/1947601911408079 · Cited by 762 · see citing works

A complex interplay between Akt, TSC2 and the two mTOR complexes

Huang, J., & Manning, B. D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370217 · Cited by 724 · see citing works

Hypoxia regulates TSC1/2–mTOR signaling and tumor suppression through REDD1-mediated 14–3–3 shuttling

DeYoung, M. P., Horak, P., Sofer, A., Sgroi, D., & Ellisen, L. W. (2008) · Genes & Development · doi:10.1101/gad.1617608 · Cited by 710 · see citing works

Targeting protein prenylation for cancer therapy

Berndt, N., Hamilton, A. D., & Sebti, S. M. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3151 · Cited by 614 · see citing works

TBC1D7 Is a Third Subunit of the TSC1-TSC2 Complex Upstream of mTORC1

Dibble, C. C., Elis, W., Menon, S., Qin, W., Klekota, J., Asara, J. M., Finan, P. M., Kwiatkowski, D. J., Murphy, L. O., & Manning, B. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.009 · Cited by 612 · see citing works

The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4

Csibi, A., Fendt, S.-M., Li, C., Poulogiannis, G., Choo, A. Y., Chapski, D. J., Jeong, S. M., Dempsey, J. M., Parkhitko, A., Morrison, T., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.023 · Cited by 586 · see citing works

Mammalian target of rapamycin up-regulation of pyruvate kinase isoenzyme type M2 is critical for aerobic glycolysis and tumor growth

Sun, Q., Chen, X., Ma, J., Peng, H., Wang, F., Zha, X., Wang, Y., Jing, Y., Yang, H., Chen, R., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014769108 · Cited by 586 · see citing works

The macrophage switch in obesity development

Castoldi, A., Naffah de Souza, C., Câmara, N. O. S., & Moraes-Vieira, P. M. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00637 · Cited by 575 · see citing works

Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity

Hahn-Windgassen, A., Nogueira, V., Chen, C.-C., Skeen, J. E., Sonenberg, N., & Hay, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502876200 · Cited by 539 · see citing works

TSC2 regulates VEGF through mTOR-dependent and -independent pathways

Brugarolas, J. B., Vazquez, F., Reddy, A., Sellers, W. R., & Kaelin, W. G. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00187-9 · Cited by 528 · see citing works

Regulation of neuronal morphology and function by the tumor suppressors Tsc1 and Tsc2

Tavazoie, S. F., Alvarez, V. A., Ridenour, D. A., Kwiatkowski, D. J., & Sabatini, B. L. (2005) · Nature Neuroscience · doi:10.1038/nn1566 · Cited by 497 · see citing works

mTOR: Role in cancer, metastasis and drug resistance

Murugan, A. K. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.07.003 · Cited by 483 · see citing works

Pharmacological Inhibition of mTORC1 Suppresses Anatomical, Cellular, and Behavioral Abnormalities in Neural-Specific<i>Pten</i>Knock-Out Mice

Zhou, J., Blundell, J., Ogawa, S., Kwon, C.-H., Zhang, W., Sinton, C., Powell, C. M., & Parada, L. F. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5685-08.2009 · Cited by 441 · see citing works

Next-generation mTOR inhibitors in clinical oncology: how pathway complexity informs therapeutic strategy

Wander, S. A., Hennessy, B. T., & Slingerland, J. M. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44145 · Cited by 427 · see citing works

4E-BP1 Is a Key Effector of the Oncogenic Activation of the AKT and ERK Signaling Pathways that Integrates Their Function in Tumors

She, Q.-B., Halilovic, E., Ye, Q., Zhen, W., Shirasawa, S., Sasazuki, T., Solit, D. B., & Rosen, N. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.023 · Cited by 400 · see citing works

Progeria syndromes and ageing: what is the connection?

Burtner, C. R., & Kennedy, B. K. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2944 · Cited by 386 · see citing works

Rheb Binds Tuberous Sclerosis Complex 2 (TSC2) and Promotes S6 Kinase Activation in a Rapamycin- and Farnesylation-dependent Manner

Castro, A. F., Rebhun, J. F., Clark, G. J., & Quilliam, L. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300226200 · Cited by 381 · see citing works

Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning

Cai, S.-L., Tee, A. R., Short, J. D., Bergeron, J. M., Kim, J., Shen, J., Guo, R., Johnson, C. L., Kiguchi, K., & Walker, C. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200507119 · Cited by 359 · see citing works

Oncogenic Roles of the PI3K/AKT/mTOR axis

Aoki, M., & Fujishita, T. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_6 · Cited by 355 · see citing works

Signalling pathways regulating muscle mass in ageing skeletal muscle. The role of the IGF1-Akt-mTOR-FoxO pathway

Sandri, M., Barberi, L., Bijlsma, A. Y., Blaauw, B., Dyar, K. A., Milan, G., Mammucari, C., Meskers, C. G. M., Pallafacchina, G., Paoli, A., et al. (2013) · Biogerontology · doi:10.1007/s10522-013-9432-9 · Cited by 340 · see citing works

Role of mTOR in physiology and pathology of the nervous system

Swiech, L., Perycz, M., Malik, A., & Jaworski, J. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.08.015 · Cited by 338 · see citing works

Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling

Drummond, M. J., Dreyer, H. C., Fry, C. S., Glynn, E. L., & Rasmussen, B. B. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91397.2008 · Cited by 322 · see citing works

mTOR signaling and its roles in normal and abnormal brain development

Takei, N., & Nawa, H. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00028 · Cited by 317 · see citing works

AMPK: Regulating Energy Balance at the Cellular and Whole Body Levels

Hardie, D. G., & Ashford, M. L. J. (2014) · Physiology · doi:10.1152/physiol.00050.2013 · Cited by 280 · see citing works

Increased Phosphorylation of Akt Substrate of 160 kDa (AS160) in Rat Skeletal Muscle in Response to Insulin or Contractile Activity

Bruss, M. D., Arias, E. B., Lienhard, G. E., & Cartee, G. D. (2005) · Diabetes · doi:10.2337/diabetes.54.1.41 · Cited by 273 · see citing works

Molecular Mechanisms of Autophagy in the Cardiovascular System

Gatica, D., Chiong, M., Lavandero, S., & Klionsky, D. J. (2015) · Circulation Research · doi:10.1161/circresaha.114.303788 · Cited by 272 · see citing works

ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)

Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268 · see citing works

mTORC1 Signaling under Hypoxic Conditions Is Controlled by ATM-Dependent Phosphorylation of HIF-1α

Cam, H., Easton, J. B., High, A., & Houghton, P. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.030 · Cited by 266 · see citing works

The Stress-inducted Proteins RTP801 and RTP801L Are Negative Regulators of the Mammalian Target of Rapamycin Pathway

Corradetti, M. N., Inoki, K., & Guan, K.-L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c400557200 · Cited by 237 · see citing works

Metabolic Stress Controls mTORC1 Lysosomal Localization and Dimerization by Regulating the TTT-RUVBL1/2 Complex

Kim, S. G., Hoffman, G. R., Poulogiannis, G., Buel, G. R., Jang, Y. J., Lee, K. W., Kim, B.-Y., Erikson, R. L., Cantley, L. C., Choo, A. Y., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.003 · Cited by 215 · see citing works

mTOR pathway as a target in tissue hypertrophy

Lee, C.-H., Inoki, K., & Guan, K.-L. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105359 · Cited by 179 · see citing works

Molecular mechanisms of autism: a possible role for Ca2+ signaling

Krey, J. F., & Dolmetsch, R. E. (2007) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2007.01.010 · Cited by 169 · see citing works

mTOR Is Activated in the Majority of Malignant Melanomas

Karbowniczek, M., Spittle, C. S., Morrison, T., Wu, H., & Henske, E. P. (2008) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5701074 · Cited by 168 · see citing works

Tuberous Sclerosis Complex Activity Is Required to Control Neuronal Stress Responses in an mTOR-Dependent Manner

Di Nardo, A., Kramvis, I., Cho, N., Sadowski, A., Meikle, L., Kwiatkowski, D. J., & Sahin, M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.0778-09.2009 · Cited by 165 · see citing works

Lysosomal recruitment of TSC2 is a universal response to cellular stress

Demetriades, C., Plescher, M., & Teleman, A. A. (2016) · Nature Communications · doi:10.1038/ncomms10662 · Cited by 160 · see citing works

REDD1 enhances protein phosphatase 2A-mediated dephosphorylation of Akt to repress mTORC1 signaling

Dennis, M. D., Coleman, C. S., Berg, A., Jefferson, L. S., & Kimball, S. R. (2014) · Science Signaling · doi:10.1126/scisignal.2005103 · Cited by 159 · see citing works

Are Wnt/β-Catenin and PI3K/AKT/mTORC1 Distinct Pathways in Colorectal Cancer?

Prossomariti, A., Piazzi, G., Alquati, C., & Ricciardiello, L. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.04.007 · Cited by 155 · see citing works

What a Tangled Web We Weave: Emerging Resistance Mechanisms to Inhibition of the Phosphoinositide 3-Kinase Pathway

Klempner, S. J., Myers, A. P., & Cantley, L. C. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0063 · Cited by 148 · see citing works

Mislocalization of the Cell Polarity Protein Scribble Promotes Mammary Tumorigenesis and Is Associated with Basal Breast Cancer

Feigin, M. E., Akshinthala, S. D., Araki, K., Rosenberg, A. Z., Muthuswamy, L. B., Martin, B., Lehmann, B. D., Berman, H. K., Pietenpol, J. A., Cardiff, R. D., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3415 · Cited by 135 · see citing works

<scp>TOR</scp>‐mediated regulation of metabolism in aging

Antikainen, H., Driscoll, M., Haspel, G., & Dobrowolski, R. (2017) · Aging Cell · doi:10.1111/acel.12689 · Cited by 122 · see citing works

From mTOR to cognition: molecular and cellular mechanisms of cognitive impairments in tuberous sclerosis

Ehninger, D., De Vries, P. J., & Silva, A. J. (2009) · Journal of Intellectual Disability Research · doi:10.1111/j.1365-2788.2009.01208.x · Cited by 120 · see citing works

Phosphorylation of the insulin receptor by AMP-activated protein kinase (AMPK) promotes ligand-independent activation of the insulin signalling pathway in rodent muscle

Chopra, I., Li, H. F., Wang, H., & Webster, K. A. (2012) · Diabetologia · doi:10.1007/s00125-011-2407-y · Cited by 116 · see citing works

Macropinocytosis, mTORC1 and cellular growth control

Yoshida, S., Pacitto, R., Inoki, K., & Swanson, J. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2710-y · Cited by 114 · see citing works

TSC1/TSC2 signaling in the CNS

Han, J. M., & Sahin, M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.02.001 · Cited by 105 · see citing works

Insulin‐like growth factor 1 can promote proliferation and osteogenic differentiation of human dental pulp stem cells via m<scp>TOR</scp> pathway

Feng, X., Huang, D., Lu, X., Feng, G., Xing, J., Lu, J., Xu, K., Xia, W., Meng, Y., Tao, T., et al. (2014) · Development, Growth &amp; Differentiation · doi:10.1111/dgd.12179 · Cited by 101 · see citing works

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 · see citing works

Cholesterol Biosynthesis Supports Myelin Gene Expression and Axon Ensheathment through Modulation of P13K/Akt/mTor Signaling

Mathews, E. S., & Appel, B. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0726-16.2016 · Cited by 97 · see citing works

Rheb localized on the Golgi membrane activates lysosome-localized mTORC1 at the Golgi–lysosome contact site

Hao, F., Kondo, K., Itoh, T., Ikari, S., Nada, S., Okada, M., & Noda, T. (2018) · Journal of Cell Science · doi:10.1242/jcs.208017 · Cited by 91 · see citing works

14-3-3β Binds to and Negatively Regulates the Tuberous Sclerosis Complex 2 (TSC2) Tumor Suppressor Gene Product, Tuberin

Shumway, S. D., Li, Y., & Xiong, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200499200 · Cited by 74 · see citing works

The role of the TOR pathway in mediating the link between nutrition and longevity

Lushchak, O., Strilbytska, O., Piskovatska, V., Storey, K. B., Koliada, A., & Vaiserman, A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.03.005 · Cited by 73 · see citing works

Skeletal Muscle Recovery from Disuse Atrophy: Protein Turnover Signaling and Strategies for Accelerating Muscle Regrowth

Mirzoev, T. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217940 · Cited by 65 · see citing works

Enhanced repair of UV-induced DNA damage by 1,25-dihydroxyvitamin D3 in skin is linked to pathways that control cellular energy

Rybchyn, M. S., De Silva, W. G. M., Sequeira, V. B., McCarthy, B. Y., Dilley, A. V., Dixon, K. M., Halliday, G. M., & Mason, R. S. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.11.037 · Cited by 63 · see citing works

Tuberous Sclerosis Protein 2 (TSC2) Modulates CCN4 Cytoprotection During Apoptotic Amyloid Toxicity in Microglia

Chen Shang, Y., Zhong Chong, Z., Wang, S., & Maiese, K. (2013) · Current Neurovascular Research · doi:10.2174/156720213804806007 · Cited by 61 · see citing works

Insulin Regulation of Hepatic Lipid Homeostasis

Uehara, K., Santoleri, D., Whitlock, A. E. G., & Titchenell, P. M. (2023) · Comprehensive Physiology · doi:10.1002/cphy.c220015 · Cited by 49 · see citing works

Heightening Energetic Stress Selectively Targets LKB1-Deficient Non–Small Cell Lung Cancers

Momcilovic, M., McMickle, R., Abt, E., Seki, A., Simko, S. A., Magyar, C., Stout, D. B., Fishbein, M. C., Walser, T. C., Dubinett, S. M., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-0797 · Cited by 46 · see citing works

Role of Adenosine 5′-Monophosphate-Activated Protein Kinase Subunits in Skeletal Muscle Mammalian Target of Rapamycin Signaling

Deshmukh, A. S., Treebak, J. T., Long, Y. C., Viollet, B., Wojtaszewski, J. F. P., & Zierath, J. R. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0448 · Cited by 44 · see citing works

Branched-chain amino acid fortification does not restore muscle protein synthesis rates following ingestion of lower-compared with higher-dose mycoprotein

Monteyne, A. J., Coelho, M. O., Porter, C., Abdelrahman, D. R., Jameson, T. S., Finnigan, T. J., Stephens, F. B., Dirks, M. L., & Wall, B. T. (2020) · The Journal of Nutrition · doi:10.1093/jn/nxaa251 · Cited by 29 · see citing works

RIP3 antagonizes a TSC2-mediated pro-survival pathway in glioblastoma cell death

Fettweis, G., Di Valentin, E., L'homme, L., Lassence, C., Dequiedt, F., Fillet, M., Coupienne, I., & Piette, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.014 · Cited by 26 · see citing works

Physiological and pathophysiological actions of insulin in the liver

Kubota, N., Kubota, T., & Kadowaki, T. (2025) · Endocrine Journal · doi:10.1507/endocrj.ej24-0192 · Cited by 19 · see citing works

Tumor Suppressor Gene PTEN and Gastric Tumor

Zhang, R., Jiang, X., & SaiYing, Z. (2009) · Xiandai shengwu yixue jinzhan

Tumor Suppressor PTEN is Mutated in Canine Osteosarcoma Cell Lines and Tumors

Levine, R. A., Forest, T. W., & Smith, C. (2002) · Veterinary Pathology · doi:10.1354/vp.39-3-372 · Cited by 101 · see citing works

Present investigation of PTEN gene in cardiovascular system

Xue-bo, Y. (2010) · Zhongguo bingli shengli zazhi

Research on PTEN and tumor and PTEN gene therapy

Niu, C.-G., Chai, M.-W., Xu, X., et al. (2010) · 肿瘤研究与临床 · doi:10.3760/cma.j.issn.1006-9801.2010.06.026

The tumor suppressor PTEN interacts with p53 in hereditary cancer

NAKANISHI, A., Kitagishi, Y., Ogura, Y., & Matsuda, S. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2377 · Cited by 94 · see citing works