Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex

mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery

Kim, D., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00808-5 · Cited by 3,051

Mechanism of activation of protein kinase B by insulin and IGF‐1.

Alessi, D. R., Andjelković, M., Caudwell, B., Cron, P. D., MORRICE, N. A., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,014

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

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Rictor, a Novel Binding Partner of mTOR, Defines a Rapamycin-Insensitive and Raptor-Independent Pathway that Regulates the Cytoskeleton

Sarbassov, D. D., Ali, S. M., Kim, D.-H., Guertin, D. A., Latek, R. R., Erdjument-Bromage, H., Tempst, P., & Sabatini, D. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.054 · Cited by 2,665

Two TOR Complexes, Only One of which Is Rapamycin Sensitive, Have Distinct Roles in Cell Growth Control

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

Insulin Resistance and a Diabetes Mellitus-Like Syndrome in Mice Lacking the Protein Kinase Akt2 (PKBβ)

Cho, H., Mu, J., Kim, J. K., Thorvaldsen, J. L., Chu, Q., Crenshaw, E. B., Kaestner, K. H., Bartolomei, M. S., Shulman, G. I., & Birnbaum, M. J. (2001) · Science · doi:10.1126/science.292.5522.1728 · Cited by 1,860

Raptor, a Binding Partner of Target of Rapamycin (TOR), Mediates TOR Action

Hara, K., Maruki, Y., Long, X., Yoshino, K.-I., Oshiro, N., Sujuti, H., Tokunaga, C., Avruch, J., & Yonezawa, K. (2002) · Cell · doi:10.1016/s0092-8674(02)00833-4 · Cited by 1,810

RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1

Burnett, P. E., Barrow, R. K., Cohen, N. A., Snyder, S. H., & Sabatini, D. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1432 · Cited by 1,130

The TSC1-2 tumor suppressor controls insulin–PI3K signaling via regulation of IRS proteins

Harrington, L. S., Findlay, G. M., Gray, A., Толкачева, Т. А., Wigfield, S., Rebholz, H., Barnett, J., Leslie, N. R., Cheng, S., Shepherd, P. R., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403069 · Cited by 1,123

Protein Kinase B Kinases That Mediate Phosphatidylinositol 3,4,5-Trisphosphate-Dependent Activation of Protein Kinase B

Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061

Targeting the PI3K/Akt/mTOR signaling pathway in B-precursor acute lymphoblastic leukemia and its therapeutic potential

Neri, L. M., Cani, A., Martelli, A. M., Simioni, C., Junghanß, C., Tabellini, G., Ricci, F., Tazzari, P. L., Pagliaro, P., McCubrey, J. A., et al. (2013) · Leukemia · doi:10.1038/leu.2013.226 · Cited by 136

Molecular imaging of Akt kinase activity

Zhang, L., Lee, K. C., Bhojani, M. S., Khan, A. P., Shilman, A., Holland, E. C., Ross, B. D., & Rehemtulla, A. (2007) · Nature Medicine · doi:10.1038/nm1608 · Cited by 137

The PI3K/Akt pathway: a critical player in intervertebral disc degeneration

Ouyang, Z., Wang, W.-J., Yan, Y., Wang, B., & Lv, G. (2017) · Oncotarget · doi:10.18632/oncotarget.18628 · Cited by 136

Competitive glucose metabolism as a target to boost bladder cancer immunotherapy

Afonso, J., Santos, L. L., Longatto‐Filho, A., & Baltazar, F. (2020) · Nature Reviews Urology · doi:10.1038/s41585-019-0263-6 · Cited by 138

KRAS-regulated glutamine metabolism requires UCP2-mediated aspartate transport to support pancreatic cancer growth

Raho, S., Capobianco, L., Malivindi, R., Vozza, A., Piazzolla, C., Leonardis, F. D., Gorgoglione, R., Scarcia, P., Pezzuto, F., Agrimi, G., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00315-1 · Cited by 138

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

Skeletal Muscle Abnormalities in Heart Failure

Kinugawa, S., Takada, S., Matsushima, S., Okita, K., & Tsutsui, H. (2015) · International Heart Journal · doi:10.1536/ihj.15-108 · Cited by 140

Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2

Niles, B. J., Mogri, H., Hill, A., Vlahakis, A., & Powers, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117563109 · Cited by 134

The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling

Hussain, S., Foreman, O., Perkins, S. L., Witzig, T. E., Miles, R. R., van Deursen, J., & Galardy, P. J. (2010) · Leukemia · doi:10.1038/leu.2010.138 · Cited by 137

Adiponectin-Activated AMPK Stimulates Dephosphorylation of AKT through Protein Phosphatase 2A Activation

Kim, K.-Y., Baek, A., Hwang, J.-E., Choi, Y. A., Jeong, J., Lee, M.-S., Cho, D. H., Lim, J., Kim, K. I., & Yang, Y. D. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2641 · Cited by 139

DND1 maintains germline stem cells via recruitment of the CCR4–NOT complex to target mRNAs

Yamaji, M., Jishage, M., Meyer, C., Suryawanshi, H., Der, E. B., Yamaji, M., Garzia, A., Morozov, P. S., Manickavel, S., McFarland, H. L., et al. (2017) · Nature · doi:10.1038/nature21690 · Cited by 136

Vasculogenesis and angiogenesis initiation under normoxic conditions through Wnt/β-catenin pathway in gliomas

Vallée, A., Guillevin, R., & Vallée, J.-N. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0032 · Cited by 137

Inhibition of mTORC1 by lncRNA H19 via disrupting 4E-BP1/Raptor interaction in pituitary tumours

Wu, Z. R., Yan, L., Liu, Y. T., Cao, L., Guo, Y., Zhang, Y., Yao, H., Cai, L., Shang, H. B., Rui, W. W., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06853-3 · Cited by 135

The TSC-mTOR Pathway Mediates Translational Activation of TOP mRNAs by Insulin Largely in a Raptor- or Rictor-Independent Manner

Patursky-Polischuk, I., Stolovich-Rain, M., Hausner-Hanochi, M., Kasir, J., Cybulski, N., Avruch, J., Rüegg, M. A., Hall, M. N., & Meyuhas, O. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00980-08 · Cited by 139

Re-evaluating AKT regulation: role of TOR complex 2 in tissue growthPreprint

Hietakangas, V., & Cohen, S. M. (2007) · Genes & Development · doi:10.1101/gad.416307 · Cited by 134

Amino Acid Signaling to MTOR Mediated by Inositol Polyphosphate Multikinase

Kim, S., Kim, S. F., Maag, D., Maxwell, M. J., Resnick, A. C., Juluri, K. R., Chakraborty, A., Koldobskiy, M. A., Cha, S. H., Barrow, R., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.007 · Cited by 144

GTPase Activity and Neuronal Toxicity of Parkinson's Disease–Associated LRRK2 Is Regulated by ArfGAP1

Stafa, K., Trancikova, A., Webber, P. J., Glauser, L., West, A. B., & Moore, D. J. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002526 · Cited by 127

Targeting glycogen synthase kinase-3 (GSK-3) in the treatment of Type 2 diabetes

MacAulay, K., & Woodgett, J. R. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.10.1265 · Cited by 140

mTOR Complex Component Rictor Interacts with PKCζ and Regulates Cancer Cell Metastasis

Zhang, F., Zhang, X., Li, M., Chen, P., Zhang, B., Guo, H. B., Cao, W., Wei, X., Cao, X., Hao, X., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0207 · Cited by 134

HDAC inhibition impedes epithelial–mesenchymal plasticity and suppresses metastatic, castration-resistant prostate cancer

Ruscetti, M. A., Dadashian, E. L., Guo, W., Quach, B., Mulholland, D. J., Park, J. W., Tran, L. M., Kobayashi, N., Bianchi-Frias, D., Xing, Y., et al. (2015) · Oncogene · doi:10.1038/onc.2015.444 · Cited by 133

New Insights into Protein Kinase B/Akt Signaling: Role of Localized Akt Activation and Compartment-Specific Target Proteins for the Cellular Radiation Response

Szymonowicz, K., Oeck, S., Malewicz, N. M., & Jendrossek, V. (2018) · Cancers · doi:10.3390/cancers10030078 · Cited by 135

An Akt-dependent Increase in Canonical Wnt Signaling and a Decrease in Sclerostin Protein Levels Are Involved in Strontium Ranelate-induced Osteogenic Effects in Human Osteoblasts

Rybchyn, M. S., Slater, M., Conigrave, A. D., & Mason, R. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.251116 · Cited by 132

Role of mTORC1 in mechanically induced increases in translation and skeletal muscle mass

Goodman, C. A. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01011.2018 · Cited by 133

The emerging role of the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin signaling network in normal myelopoiesis and leukemogenesis

Martelli, A. M., Evangelisti, C., Chiarini, F., Grimaldi, C., Cappellini, A., Ognibene, A., & McCubrey, J. A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.04.005 · Cited by 134

Platinum resistance in breast and ovarian cancer cell lines

Eckstein, N. (2011) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-30-91 · Cited by 138

mTORC2 sustains thermogenesis via Akt‐induced glucose uptake and glycolysis in brown adipose tissue

Albert, V., Svensson, K., Shimobayashi, M., Colombi, M., MUÑOZ, S. A., Jiménez, V., Handschin, C., Bosch, F., & Hall, M. N. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505610 · Cited by 134

Insulin signalling promotes dendrite and synapse regeneration and restores circuit function after axonal injury

Agostinone, J., Alarcon-Martinez, L., Gamlin, C., Yu, W.-Q., Wong, R. O. L., & Di Polo, A. (2018) · Brain · doi:10.1093/brain/awy142 · Cited by 124

M. tuberculosis PknG manipulates host autophagy flux to promote pathogen intracellular survival

Ge, P., Lei, Z., Yu, Y., Lu, Z., Qiang, L., Chai, Q., Zhang, Y., Zhao, D., Li, B., Pang, Y., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.1938912 · Cited by 132

Enhanced c-Met activity promotes G-CSF–induced mobilization of hematopoietic progenitor cells via ROS signaling

Tesio, M., Golan, K., Corso, S., Giordano, S., Schajnovitz, A., Vagima, Y., Shivtiel, S., Kalinkovich, A., Caione, L., Gammaitoni, L., et al. (2010) · Blood · doi:10.1182/blood-2009-06-230359 · Cited by 134

Activation of Mammalian Target of Rapamycin and Synaptogenesis: Role in the Actions of Rapid-Acting Antidepressants

Dwyer, J. M., & Duman, R. S. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2012.11.011 · Cited by 139

mTOR controls lysosome tubulation and antigen presentation in macrophages and dendritic cells

Sarić, A., Hipolito, V. E. B., Kay, J. G., Canton, J., Antonescu, C. N., & Botelho, R. J. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-05-0272 · Cited by 127

Cryo-EM structure of human mTOR complex 2

Chen, X., Liu, M., Tian, Y., Li, J., Qi, Y., Zhao, D., Wu, Z., Huang, M., Wong, C. C. L., Wang, H., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0029-3 · Cited by 138

Oxidative Stress in Methylmercury-Induced Cell Toxicity

dos Santos, A. A., Ferrer, B., Gonçalves, F. M., Tsatsakis, A. M., Renieri, E. A., Skalny, A. V., Farina, M., da Rocha, J. B. T., & Aschner, M. (2018) · Toxics · doi:10.3390/toxics6030047 · Cited by 136

The PI3K/AKT signaling pathway in cancer: Molecular mechanisms and possible therapeutic interventions

Khezri, M. R., Jafari, R., Yousefi, K., & Zolbanin, N. M. (2022) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2022.104787 · Cited by 137

ATM protein kinase mediates full activation of Akt and regulates glucose transporter 4 translocation by insulin in muscle cells

Halaby, M., Hibma, J. C., He, J., & Yang, D. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.04.011 · Cited by 137

The atypical PKCs in inflammation: NF‐κB and beyond

Díaz-Meco, M. T., & Moscat, J. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01093.x · Cited by 132

AKT Signaling in Physiology and Disease

Vasudevan, K. M., & Garraway, L. A. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_66 · Cited by 135

The PI3K, Metabolic, and Autophagy Networks: Interactive Partners in Cellular Health and Disease

Shanware, N. P., Bray, K., & Abraham, R. T. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134717 · Cited by 136

Regulation of chemotaxis by the orchestrated activation of Ras, PI3K, and TOR

Sasaki, A. T., & Firtel, R. (2006) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2006.04.007 · Cited by 133

Stress-Activated NRF2-MDM2 Cascade Controls Neoplastic Progression in Pancreas

Todoric, J., Antonucci, L., Caro, G. D., Li, N., Wu, X., Lytle, N. K., Dhar, D., Banerjee, S., Fagman, J. B., Browne, C. D., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.10.011 · Cited by 129

FoxO transcription factors in cancer metabolism

Yadav, R. K., Chauhan, A. S., Zhuang, L., & Gan, B. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.01.004 · Cited by 138

Ubiquitination of Rheb governs growth factor-induced mTORC1 activation

Deng, L., Chen, L., Zhao, L., Xu, Y., Peng, X.-P., Wang, X., Ding, L., Jin, J., Teng, H., Wang, Y., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0120-9 · Cited by 133

Targeting Akt in cancer therapy

LoPiccolo, J., Granville, C. A., Gills, J. J., & Dennis, P. A. (2007) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e3280cc2c6f · Cited by 129

The endosymbiontWolbachiaincreases insulin/IGF-like signalling inDrosophila

Ikeya, T., Broughton, S. J., Alic, N., Grandison, R. C., & Partridge, L. (2009) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2009.0778 · Cited by 139

AS160 phosphorylation is associated with activation of α 2 β 2 γ 1 - but not α 2 β 2 γ 3 -AMPK trimeric complex in skeletal muscle during exercise in humans

Treebak, J. T., Birk, J. B., Rose, A. J., Kiens, B., Richter, E. A., & Wojtaszewski, J. F. P. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00380.2006 · Cited by 133

mTOR inhibitors in the treatment of cancer

Fasolo, A., & Sessa, C. (2008) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.17.11.1717 · Cited by 132

TOR‐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

TGF-β1 Protects against Mesangial Cell Apoptosis via Induction of Autophagy

Ding, Y., Kim, J. K., Kim, S. I., Na, H.-J., Jun, S. Y., Lee, S., & Choi, M. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.093724 · Cited by 130

mTOR inhibitors in renal cell carcinoma

Battelli, C., & Cho, D. C. (2011) · Therapy · doi:10.2217/thy.11.32 · Cited by 136

Turning Off AKT: PHLPP as a Drug Target

Newton, A. C., & Trotman, L. C. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140338 · Cited by 135

ASCT2 silencing regulates mammalian target-of-rapamycin growth and survival signaling in human hepatoma cells

Fuchs, B. C., Finger, R., Onan, M. C., & Bode, B. P. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00330.2006 · Cited by 137

An emerging role for TOR signaling in mammalian tissue and stem cell physiology

Russell, R. C., Fang, C., & Guan, K. (2011) · Development · doi:10.1242/dev.058230 · Cited by 136

Mitotic Exit and Separation of Mother and Daughter Cells

Weiss, E. L. (2012) · Genetics · doi:10.1534/genetics.112.145516 · Cited by 136

Ras-mediated activation of the TORC2–PKB pathway is critical for chemotaxis

Cai, H., Das, S., Kamimura, Y., Yu, L., Parent, C. A., & Devreotes, P. N. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001129 · Cited by 127

Sarm1, a negative regulator of innate immunity, interacts with syndecan-2 and regulates neuronal morphology

Chen, C.-Y., Lin, C.-W., Chang, C.-Y., Jiang, S., & Hsueh, Y. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201008050 · Cited by 130

Multi-mechanisms are involved in reactive oxygen species regulation of mTORC1 signaling

Li, M., Zhao, L., Liu, J., Liu, A., Jia, C., Ma, D., Jiang, Y., & Bai, X. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.05.015 · Cited by 132

The possible role of the Akt signaling pathway in schizophrenia

Zheng, W., Wang, H., Zeng, Z., Lin, J., Little, P. J., Srivastava, L. K., & Quirion, R. (2012) · Brain Research · doi:10.1016/j.brainres.2012.06.032 · Cited by 130

The role of FKBP5 in cancer aetiology and chemoresistance

Li, L., Lou, Z., & Wang, L. (2010) · British Journal of Cancer · doi:10.1038/sj.bjc.6606014 · Cited by 129

The Interaction of Akt with APPL1 Is Required for Insulin-stimulated Glut4 Translocation

Saito, T., Jones, C. C., Huang, S., Czech, M., & Pilch, P. F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704150200 · Cited by 130

The podocyte as a direct target of immunosuppressive agents

Schönenberger, E., Ehrich, J. H. H., Haller, H. G., & Schiffer, M. (2010) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfq617 · Cited by 129

Merkel cell polyomavirus recruits MYCL to the EP400 complex to promote oncogenesis

Cheng, J., Park, D. E., Berrios, C. J., White, E. A., Arora, R., Yoon, R., Branigan, T. B., Xiao, T., Westerling, T., Alexander Joel Federation, et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006668 · Cited by 136

Advances in Targeting Human Epidermal Growth Factor Receptor-2 Signaling for Cancer Therapy

Meric‐Bernstam, F., & Hung, M. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1732 · Cited by 129

Effective in vivo targeting of the mammalian target of rapamycin pathway in malignant peripheral nerve sheath tumors

Johansson, G., Mahller, Y. Y., Collins, M. H., Kim, M., Nobukuni, T., Perentesis, J. P., Cripe, T. P., Lane, H. A., Kozma, S. C., Thomas, G., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2335 · Cited by 131

Genome‐wide dFOXO targets and topology of the transcriptomic response to stress and insulin signalling

Alic, N., Andrews, T. D., Giannakou, M. E., Papatheodorou, I., Slack, C., Hoddinott, M. P., Cochemé, H. M., Schuster, E. F., Thornton, J. M., & Partridge, L. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.36 · Cited by 128

Anticancer strategies based on the metabolic profile of tumor cells: therapeutic targeting of the Warburg effect

Chen, X., Li, L.-Y., Guan, Y.-D., Yang, J., & Cheng, Y. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.47 · Cited by 129

Role of Mitochondria-Associated ER Membranes in Calcium Regulation in Cancer-Specific Settings

Morciano, G., Marchi, S., Morganti, C., Sbano, L., Bittremieux, M., Kerkhofs, M., Corricelli, M., Danese, A., Karkucińska‐Więckowska, A., Wieckowski, M. R., et al. (2018) · Neoplasia · doi:10.1016/j.neo.2018.03.005 · Cited by 136

The Long Noncoding RNA Cancer Susceptibility 9 and RNA Binding Protein Heterogeneous Nuclear Ribonucleoprotein L Form a Complex and Coregulate Genes Linked to AKT Signaling

Klingenberg, M., Groß, M., Goyal, A., Polycarpou‐Schwarz, M., Miersch, T., Ernst, A., Leupold, J. H., Patil, N., Warnken, U. H., Allgayer, H., et al. (2018) · Hepatology · doi:10.1002/hep.30102 · Cited by 128

MicroRNAs and the PTEN/PI3K/Akt pathway in gastric cancer (Review)

Hu, M., Zhu, S., Xiong, S., Xue, X., & Zhou, X. (2019) · Oncology Reports · doi:10.3892/or.2019.6962 · Cited by 128

mTORC1 Activation Regulates β-Cell Mass and Proliferation by Modulation of Cyclin D2 Synthesis and Stability

Balcázar, N., Sathyamurthy, A., Elghazi, L., Gould, A. P., Weiss, A., Shiojima, I., Walsh, K. X., & Bernal‐Mizrachi, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807458200 · Cited by 126

Myeloid-Specific Rictor Deletion Induces M1 Macrophage Polarization and Potentiates In Vivo Pro-Inflammatory Response to Lipopolysaccharide

Festuccia, W. T., Pouliot, P., Bakan, I., Sabatini, D. M., & Laplante, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095432 · Cited by 103

Rheb1 Is Required for mTORC1 and Myelination in Postnatal Brain Development

Zou, J., Zhou, L., Du, X.-X., Ji, Y.-F., Xu, J., Tian, J., Jiang, W., Zou, Y., Yu, S., Gan, L., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.11.020 · Cited by 127

Compensatory activation of Akt in response to mTOR and Raf inhibitors – A rationale for dual-targeted therapy approaches in neuroendocrine tumor disease

Zitzmann, K., von Rüden, J., Brand, S., Göke, B., Lichtl, J., Spöttl, G., & Auernhammer, C. J. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.02.018 · Cited by 127

PHLPP-1 Negatively Regulates Akt Activity and Survival in the Heart

Miyamoto, S., Purcell, N. H., Smith, J. M., Gao, T., Whittaker, R., Huang, K., Castillo, R., Glembotski, C. C., Sussman, M. A., Newton, A. C., et al. (2010) · Circulation Research · doi:10.1161/circresaha.109.215020 · Cited by 127

Role of mTOR Signaling in Tumor Microenvironment: An Overview

Conciatori, F., Bazzichetto, C., Falcone, I., Pilotto, S., Bria, E., Cognetti, F., Milella, M., & Ciuffreda, L. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082453 · Cited by 131

Displacement of WDR5 from Chromatin by a WIN Site Inhibitor with Picomolar Affinity

Aho, E. R., Wang, J., Gogliotti, R. D., Howard, G. C., Phan, J., Acharya, P., Macdonald, J. D., Cheng, K. C.-C., Lorey, S. L., Lu, B., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.047 · Cited by 120

The role of mitochondria-associated membranes in cellular homeostasis and diseases

Perrone, M., Caroccia, N., Genovese, I., Missiroli, S., Modesti, L., Pedriali, G., Vezzani, B., Vitto, V. A. M., Antenori, M., Lebiedzińska, M., et al. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.11.002 · Cited by 132

Thinking globally and acting locally with TOR

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Cell Cycle Regulation by the Nutrient-Sensing Mammalian Target of Rapamycin (mTOR) Pathway

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Constitutive reductions in mTOR alter cell size, immune cell development, and antibody production

Zhang, S., Readinger, J. A., Dubois, W., Janka-Junttila, M., Robinson, R., Pruitt, M., Bliskovsky, V., Wu, J. Z., Sakakibara, K., Patel, J. D., et al. (2010) · Blood · doi:10.1182/blood-2010-05-287821 · Cited by 130

α-Solanine induces ROS-mediated autophagy through activation of endoplasmic reticulum stress and inhibition of Akt/mTOR pathway

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Exercise-Induced Phosphorylation of the Novel Akt Substrates AS160 and Filamin A in Human Skeletal Muscle

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c-Jun N-Terminal Kinases Mediate Reactivation of Akt and Cardiomyocyte Survival After Hypoxic Injury In Vitro and In Vivo

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Ursolic acid a promising candidate in the therapeutics of breast cancer: Current status and future implications

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Lysosome Positioning Influences mTORC2 and AKT Signaling

Jia, R., & Bonifacino, J. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.05.009 · Cited by 122

The Importance of Being PI3K in the RAS Signaling Network

Cuesta, C., Arévalo-Alameda, C., & Castellano, E. (2021) · Genes · doi:10.3390/genes12071094 · Cited by 125

The Multifaceted Role of Nutrient Sensing and mTORC1 Signaling in Physiology and Aging

Fernandes, S., & Demetriades, C. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.707372 · Cited by 131

mTOR Complex-2 Activates ENaC by Phosphorylating SGK1

Lu, M., Wang, J., Jones, K. T., Ives, H. E., Feldman, M. E., Yao, L., Shokat, K. M., Ashrafi, K., & Pearce, D. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009111168 · Cited by 122

Activation of Wnt/β-Catenin Signaling Increases Insulin Sensitivity through a Reciprocal Regulation of Wnt10b and SREBP-1c in Skeletal Muscle Cells

Abiola, M., Favier, M., Christodoulou‐Vafeiadou, E., Pichard, A., Martelly, I., & Guillet-Deniau, I. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008509 · Cited by 124

Mammalian Target of Rapamycin (mTor) Mediates Tau Protein Dyshomeostasis

Tang, Z., Bereczki, E., Zhang, H., Wang, S., Li, C., Ji, X., Branca, R. M., Lehtiö, J., Guan, Z., Filipčík, P., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.435123 · Cited by 124

d-alpha-tocopheryl polyethylene glycol succinate (TPGS) induces cell cycle arrest and apoptosis selectively in Survivin-overexpressing breast cancer cells

Neophytou, C. M., Constantinou, C., Papageorgis, P., & Constantinou, A. I. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.02.003 · Cited by 125

TGF-β Induces Acetylation of Chromatin and of Ets-1 to Alleviate Repression of miR-192 in Diabetic Nephropathy

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Identification of an oncogenic RAB protein

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A chemical screen in diverse breast cancer cell lines reveals genetic enhancers and suppressors of sensitivity to PI3K isotype-selective inhibition

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The level of AKT phosphorylation on threonine 308 but not on serine 473 is associated with high-risk cytogenetics and predicts poor overall survival in acute myeloid leukaemia

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mTORC2 Regulates Cardiac Response to Stress by Inhibiting MST1

Sciarretta, S., Zhai, P., Maejima, Y., Re, D. P. D., Nagarajan, N., Yee, D., Liu, T., Magnuson, M. A., Volpe, M., Frati, G., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.010 · Cited by 127

Ubiquitin-dependent Regulation of Phospho-AKT Dynamics by the Ubiquitin E3 Ligase, NEDD4-1, in the Insulin-like Growth Factor-1 Response

Fan, C.-D., Lum, M. A., Xu, C., Black, J. D., & Wang, X. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.416339 · Cited by 122

FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade

Kuchay, S., Duan, S., Schenkein, E., Peschiaroli, A., Saraf, A., Florens, L. A., Washburn, M. P., & Pagano, M. (2013) · Nature Cell Biology · doi:10.1038/ncb2731 · Cited by 125

Signaling Events Downstream of Mammalian Target of Rapamycin Complex 2 Are Attenuated in Cells and Tumors Deficient for the Tuberous Sclerosis Complex Tumor Suppressors

Huang, J., Wu, S., Wu, C., & Manning, B. D. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0975 · Cited by 123

Central insulin and leptin-mediated autonomic control of glucose homeostasis

Marino, J. S., Xu, Y., & Hill, J. W. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2011.03.001 · Cited by 129

Loss of mTOR repressors Tsc1 or Pten has divergent effects on excitatory and inhibitory synaptic transmission in single hippocampal neuron cultures

Weston, M. C., Chen, H., & Swann, J. W. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00001 · Cited by 123

Getting In on the Akt

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Receptor-Specific Mechanisms Regulate Phosphorylation of AKT at Ser473: Role of RICTOR in b1 Integrin-Mediated Cell

Riaz, A., Zeller, K. S., & Johansson, S. (2012)

Rictor Phosphorylation on the Thr-1135 Site Does Not Require Mammalian Target of Rapamycin Complex 2

Boulbés, D. R., Chen, C.-H., Shaiken, T. E., Agarwal, N., Peterson, T. R., Addona, T. A., Keshishian, H., Carr, S. A., Magnuson, M. A., Sabatini, D. M., et al. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0409 · Cited by 67

Receptor-Specific Mechanisms Regulate Phosphorylation of AKT at Ser473: Role of RICTOR in β1 Integrin-Mediated Cell Survival

Riaz, A., Zeller, K. S., & Johansson, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032081 · Cited by 46

Regulation and functions of protein kinase B in DNA damage signaling

Bozulic, L. (2009) · edoc (University of Basel) · doi:10.5451/unibas-005031495