Coordinate regulation of ribosome biogenesis and function by the ribosomal protein S6 kinase, a key mediator of mTOR function

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216

Upstream and downstream of mTOR

Hay, N., & Sonenberg, N. (2004) · Genes & Development · doi:10.1101/gad.1212704 · Cited by 4,181

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

TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling

Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083

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 3,072

The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1

Hanks, S. K., & Hunter, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.8.7768349 · Cited by 2,828

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

Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.

Hanks, S. K., & Hunter, T. R. (1995) · PubMed · Cited by 2,518

Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB

Sarbassov, D. D., Ali, S. M., Sengupta, S., Sheen, J.-H., Hsu, P. P., Bagley, A. F., Markhard, A. L., & Sabatini, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.029 · Cited by 2,365

Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive

Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097

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

The lysosome as a cellular centre for signalling, metabolism and quality control

Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920

The mTOR Signalling Pathway in Human Cancer

Pópulo, H., Lopes, J. M., & Soares, P. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13021886 · Cited by 830

Targeting the mTOR Signaling Network for Cancer Therapy

Meric‐Bernstam, F., & Gonzalez-Angulo, A. M. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.20.0766 · Cited by 640

The life of a cell: apoptosis regulation by the PI3K/PKB pathway

Duronio, V. (2008) · Biochemical Journal · doi:10.1042/bj20081056 · Cited by 403

The TOR pathway comes of age

Stanfel, M. N., Shamieh, L. S., Kaeberlein, M. R., & Kennedy, B. K. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.007 · Cited by 347

Akt Signals through the Mammalian Target of Rapamycin Pathway to Regulate CNS Myelination

Narayanan, S. P., Flores, A. I., Wang, F., & Macklin, W. B. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0232-09.2009 · Cited by 328

Role of mTOR in anticancer drug resistance: Perspectives for improved drug treatment

Jiang, B., & Liu, L.-Z. (2008) · Drug Resistance Updates · doi:10.1016/j.drup.2008.03.001 · Cited by 249

The S6K protein family in health and disease

Tavares, M. R., Pavan, I. C. B., do Amaral, C. L., Meneguello, L., Luchessi, A. D., & Simabuco, F. M. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.03.001 · Cited by 252

Myocardial AKT: The Omnipresent Nexus

Sussman, M. A., Völkers, M., Fischer, K. M., Bailey, B., Cottage, C. T., Din, S., Gude, N. A., Avitabile, D., Alvarez, R., Sundararaman, B., et al. (2011) · Physiological Reviews · doi:10.1152/physrev.00024.2010 · Cited by 237

Targeting the PI3-Kinase/Akt/mTOR Signaling Pathway

Hassan, B., Akçakanat, A., Holder, A. M., & Meric‐Bernstam, F. (2013) · Surgical Oncology Clinics of North America · doi:10.1016/j.soc.2013.06.008 · Cited by 230

Targeting the nucleolus for cancer intervention

Quin, J. E., Devlin, J. R., Cameron, D. P., Hannan, K. M., Pearson, R. B., & Hannan, R. D. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.12.009 · Cited by 230

Potential Targets for Prevention of Colorectal Cancer: a Focus on PI3K/Akt/mTOR and Wnt Pathways

Pandurangan, A. K. (2013) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2013.14.4.2201 · Cited by 198

The Human Papillomavirus Type 16 E6 Oncoprotein Activates mTORC1 Signaling and Increases Protein Synthesis

Spangle, J. M., & Münger, K. (2010) · Journal of Virology · doi:10.1128/jvi.00974-10 · Cited by 204

AGC protein kinases: From structural mechanism of regulation to allosteric drug development for the treatment of human diseases

Arencibia, J. M., Pastor‐Flores, D., Bauer, A. F., Schulze, J. O., & Biondi, R. M. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.010 · Cited by 189

Mechanisms Limiting Body Growth in Mammals

Lui, J. C. K., & Baron, J. (2011) · Endocrine Reviews · doi:10.1210/er.2011-0001 · Cited by 170

Glycogen synthase kinase (GSK)-3 promotes p70 ribosomal protein S6 kinase (p70S6K) activity and cell proliferation

Shin, S., Wolgamott, L., Yu, Y., Blenis, J., & Yoon, S.-O. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110195108 · Cited by 169

Second AKT: The rise of SGK in cancer signalling

Bruhn, M. A., Pearson, R. B., Hannan, R. D., & Sheppard, K. E. (2010) · Growth Factors · doi:10.3109/08977194.2010.518616 · Cited by 162

Translational Control during Endoplasmic Reticulum Stress beyond Phosphorylation of the Translation Initiation Factor eIF2α

Guan, B., Krokowski, D., Majumder, M., Schmotzer, C. L., Kimball, S. R., Merrick, W. C., Koromilas, A. E., & Hatzoglou, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.543215 · Cited by 161

Acute resistance exercise activates rapamycin‐sensitive and ‐insensitive mechanisms that control translational activity and capacity in skeletal muscle

West, D. W. D., Baehr, L. M., Marcotte, G. R., Chason, C. M., Tolento, L., Gomes, A. V., Bodine, S. C., & Baar, K. (2015) · The Journal of Physiology · doi:10.1113/jp271365 · Cited by 152

Testosterone Signals through mTOR and Androgen Receptor to Induce Muscle Hypertrophy

Basualto-Alarcón, C., Jorquera, G., Altamirano, F. J., Jaimovich, E., & Estrada, M. (2013) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31828cf5f3 · Cited by 158

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

The Role of mTORC1 in Regulating Protein Synthesis and Skeletal Muscle Mass in Response to Various Mechanical Stimuli

Goodman, C. A. (2013) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2013_17 · Cited by 145

Deciphering the Role of PI3K/Akt/mTOR Pathway in Breast Cancer Biology and Pathogenesis

McAuliffe, P. F., Meric‐Bernstam, F., Mills, G. B., & Gonzalez-Angulo, A. M. (2010) · Clinical Breast Cancer · doi:10.3816/cbc.2010.s.013 · Cited by 136

mTOR inhibitors in renal cell carcinoma

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

Combination Therapy Targeting Ribosome Biogenesis and mRNA Translation Synergistically Extends Survival in MYC-Driven Lymphoma

Devlin, J. R., Hannan, K. M., Hein, N., Cullinane, C. M., Kusnadi, E. P., Ng, P. Y., George, A. J., Shortt, J., Bywater, M. J., Poortinga, G., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0673 · Cited by 126

Temporal Coding of Insulin Action through Multiplexing of the AKT Pathway

Kubota, H., Noguchi, R., Toyoshima, Y., Ozaki, Y.-I., Uda, S., Watanabe, K., Ogawa, W., & Kuroda, S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.018 · Cited by 123

Estrogen receptor β ligand therapy activates PI3K/Akt/mTOR signaling in oligodendrocytes and promotes remyelination in a mouse model of multiple sclerosis

Kumar, S., Patel, R., Moore, S. M., Crawford, D. K., Suwanna, N., Mangiardi, M., & Tiwari-Woodruff, S. K. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.04.005 · Cited by 129

A Critical Kinase Cascade In Neurological Disorders: Pi3K, Akt and Mtor

Chong, Z. Z., Shang, Y., Wang, S., & Maiese, K. (2012) · Future Neurology · doi:10.2217/fnl.12.72 · Cited by 122

JAK2V617F negatively regulates p53 stabilization by enhancing MDM2 via La expression in myeloproliferative neoplasms

Nakatake, M., Monte-Mór, B. D. C. R., Debili, N., Casadevall, N., Ribrag, V., Solary, É., Vainchenker, W., & Plo, I. (2011) · Oncogene · doi:10.1038/onc.2011.313 · Cited by 120

Shedding new light on neurodegenerative diseases through the mammalian target of rapamycin

Chong, Z. Z., Shang, Y. C., Wang, S., & Maiese, K. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.08.001 · Cited by 119

Therapeutic targeting of the mTOR ‐signalling pathway in cancer: benefits and limitations

Moschetta, M., Reale, A., Marasco, C., Vacca, A., & Carratù, M. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12749 · Cited by 119

Unique translation initiation of mRNAs-containing TISU element

Elfakess, R., Sinvani, H., Haimov, O., Svitkin, Y. V., Sonenberg, N., & Dikstein, R. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr484 · Cited by 115

Diverse Regulators of Human Ribosome Biogenesis Discovered by Changes in Nucleolar Number

Farley‐Barnes, K. I., McCann, K. L., Ogawa, L. M., Merkel, J., Surovtseva, Y. V., & Baserga, S. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.056 · Cited by 116

Prion protein interaction with stress-inducible protein 1 enhances neuronal protein synthesis via mTOR

Roffé, M., Beraldo, F. H., Bester, R., Nunziante, M., Bach, C., Mancini, G. L., Gilch, S., Vorberg, I. M., Castilho, B. A., Martins, V. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000784107 · Cited by 111

Mechanisms of Resistance to PI3K Inhibitors in Cancer: Adaptive Responses, Drug Tolerance and Cellular Plasticity

Wright, S. C. E., Vasilevski, N., Serra, V., Rodon, J. A., & Eichhorn, P. J. A. (2021) · Cancers · doi:10.3390/cancers13071538 · Cited by 116

Oxidant Stress and Signal Transduction in the Nervous System with the PI 3-K, Akt, and mTOR Cascade

Maiese, K., Chong, Z. Z., Wang, S., & Shang, Y. C. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131113830 · Cited by 109

Constitutive Role for IRE1α-XBP1 Signaling Pathway in the Insulin-Mediated Hepatic Lipogenic Program

Ning, J., Hong, T., Ward, A. R., Pi, J., Liu, Z., Liu, H.-Y., & Cao, W. (2011) · Endocrinology · doi:10.1210/en.2010-1036 · Cited by 109

Activation of critical, host-induced, metabolic and stress pathways marks neutrophil entry into cystic fibrosis lungs

Makam, M., Diaz, D., Laval, J., Gernez, Y., Conrad, C., Dunn, C. E., Davies, Z. A., Moss, R. B., Herzenberg, L. A., Herzenberg, L. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813410106 · Cited by 104

Mammalian Target of Rapamycin Signaling Modulates Photic Entrainment of the Suprachiasmatic Circadian Clock

Cao, R., Li, A., Cho, H.-Y., Lee, B., & Obrietan, K. H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5482-09.2010 · Cited by 108

MiR-99a Antitumor Activity in Human Breast Cancer Cells through Targeting of mTOR Expression

Hu, Y., Zhu, Q., & Tang, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092099 · Cited by 102

mTOR signaling regulates the processing of pre-rRNA in human cells

Iadevaia, V., Zhang, Z., Jan, E., & Proud, C. G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1040 · Cited by 106

PI3K/AKT/PTEN pathway as a target for Crohn’s disease therapy (Review)

Tokuhira, N., Kitagishi, Y., Suzuki, M., Minami, A., NAKANISHI, A., Ono, Y., Kobayashi, K., Matsuda, S., & Ogura, Y. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1981 · Cited by 102

Glycolysis Inhibition Sensitizes Non–Small Cell Lung Cancer with T790M Mutation to Irreversible EGFR Inhibitors via Translational Suppression of Mcl-1 by AMPK Activation

Kim, S. M., Yun, M. R., Hong, Y. K., Solca, F., Kim, J.-H., Kim, H. J., & Cho, B. C. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-1188 · Cited by 100

Mammalian target of rapamycin signaling in diabetic cardiovascular disease

Chong, Z., & Maiese, K. (2012) · Cardiovascular Diabetology · doi:10.1186/1475-2840-11-45 · Cited by 95

PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer

(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93

Targeting mTOR for fighting diseases: A revisited review of mTOR inhibitors

Xu, T., Sun, D., Chen, Y., & Ouyang, L. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112391 · Cited by 97

Roles of the mammalian target of rapamycin, mTOR, in controlling ribosome biogenesis and protein synthesis

Iadevaia, V., Huo, Y., Zhang, Z., Foster, L. J., & Proud, C. G. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110682 · Cited by 93

Arginase‐II Induces Vascular Smooth Muscle Cell Senescence and Apoptosis Through p66Shc and p53 Independently of Its l ‐Arginine Ureahydrolase Activity: Implications for Atherosclerotic Plaque Vulnerability

Xiong, Y., Yu, Y., Montani, J., Yang, Z., & Ming, X. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000096 · Cited by 91

Regulation of mTOR Activity in Snell Dwarf and GH Receptor Gene-Disrupted Mice

Dominick, G., Berryman, D. E., List, E. O., Kopchick, J. J., Li, X., Miller, R. A., & Garcia, G. G. (2015) · Endocrinology · doi:10.1210/en.2014-1690 · Cited by 79

d4eBP acts downstream of both dTOR and dFoxo to modulate cardiac functional aging in Drosophila

Wessells, R. J., Fitzgerald, E., Piazza, N., Ocorr, K. A., Morley, S., Davies, C. R., Lim, H., Elmeń, L., Hayes, M., Oldham, S., et al. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00504.x · Cited by 90

Fasting Increases Human Skeletal Muscle Net Phenylalanine Release and This Is Associated with Decreased mTOR Signaling

Vendelbo, M. H., Møller, A. B., Christensen, B., Nellemann, B., Clasen, B. F., Nair, K. S., Jørgensen, J. O. L., Jessen, N., & Møller, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102031 · Cited by 90

Nutrient/TOR‐dependent regulation of RNA polymerase III controls tissue and organismal growth in Drosophila

Marshall, L., Rideout, E. J., & Grewal, S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.33 · Cited by 84

Echinococcus multilocularisas an experimental model in stem cell research and molecular host-parasite interaction

Brehm, K. (2009) · Parasitology · doi:10.1017/s0031182009991727 · Cited by 85

Taking aim at Alzheimer's disease through the mammalian target of rapamycin

Maiese, K. (2014) · Annals of Medicine · doi:10.3109/07853890.2014.941921 · Cited by 88

Inducing autophagy

Harder, L. M., Bunkenborg, J., & Andersen, J. (2013) · Autophagy · doi:10.4161/auto.26863 · Cited by 80

Monocytes present age-related changes in phospholipid concentration and decreased energy metabolism

Saare, M., Tserel, L., Haljasmägi, L., Taalberg, E., Peet, N., Eimre, M., Vetik, R., Kingo, K., Saks, K., Tamm, R., et al. (2020) · Aging Cell · doi:10.1111/acel.13127 · Cited by 79

PRAS40 Is an Integral Regulatory Component of Erythropoietin mTOR Signaling and Cytoprotection

Chong, Z. Z., Shang, Y., Wang, S., & Maiese, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045456 · Cited by 74

Neuroprotective effects of salidroside through PI3K/Akt pathway activation in Alzheimer’s disease models

Chen, S., Zhang, B., Wang, Y., Li, H., Xiong, R., Zhao, Z., Chu, X., Li, Q., & Sun, S. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s99958 · Cited by 75

A pilot ‘window of opportunity’ neoadjuvant study of metformin in localised prostate cancer

Joshua, A. M., Zannella, V. E., Downes, M. R., Bowes, B., Hersey, K. M., Koritzinsky, M., Schwab, M. G., Hofmann, U., Evans, A., van der Kwast, T., et al. (2014) · Prostate Cancer and Prostatic Diseases · doi:10.1038/pcan.2014.20 · Cited by 75

Rapamycin Regulates Stearoyl CoA Desaturase 1 Expression in Breast Cancer

Luyimbazi, D. T., Akçakanat, A., McAuliffe, P. F., Zhang, L., Singh, G., Gonzalez-Angulo, A. M., Chen, H., Do, K.-A., Zheng, Y., Hung, M., et al. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0980 · Cited by 73

Restriction of dietary protein decreases mTORC1 in tumors and somatic tissues of a tumor-bearing mouse xenograft model

Lamming, D. W., Cummings, N. E., Rastelli, A. L., Gao, F., Cava, E., Bertozzi, B., Spelta, F., Pili, R., & Fontana, L. (2015) · Oncotarget · doi:10.18632/oncotarget.5180 · Cited by 69

The skeletal muscle fiber: a mechanically sensitive cell

Olsen, L. A., Nicoll, J. X., & Fry, A. C. (2019) · European Journal of Applied Physiology · doi:10.1007/s00421-018-04061-x · Cited by 80

Clinical potential of the mTOR targets S6K1 and S6K2 in breast cancer

Pérez‐Tenorio, G., Karlsson, E. A., Waltersson, M. A., Olsson, B., Holmlund, B., Nordenskjöld, B. A., Fornander, T., Skoog, L. K., & Stål, O. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-1058-x · Cited by 69

Effects of replacing fishmeal with different cottonseed meals on growth, feed utilization, haematological indexes, intestinal and liver morphology of juvenile turbot (Scophthalmus maximusL.)

Bian, F., Zhou, H., He, G., Wang, C., Peng, H., Pu, X., Jiang, H., Wang, X., & Mai, K. (2017) · Aquaculture Nutrition · doi:10.1111/anu.12518 · Cited by 63

Regulation of mTORC1 by amino acids in mammalian cells: A general picture of recent advances

Zhang, S., Lin, X., Hou, Q., Hu, Z., Wang, Y., & Wang, Z. (2021) · Animal nutrition · doi:10.1016/j.aninu.2021.05.003 · Cited by 68

Focal adhesion kinase is a load‐dependent governor of the slow contractile and oxidative muscle phenotype

Durieux, A., D’Antona, G., Dominique Desplanches, C., Freyssenet, D. G., Klossner, S., Bottinelli, R., & Flück, M. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.171355 · Cited by 62

iTRAQ-based comparative proteomic analysis of Vero cells infected with virulent and CV777 vaccine strain-like strains of porcine epidemic diarrhea virus

Guo, X., Hu, H., Chen, F., Li, Z., Ye, S., Cheng, S., Zhang, M., & He, Q. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.09.002 · Cited by 60

Cutting through the Complexities of mTOR for the Treatment of Stroke

Maiese, K. (2014) · Current Neurovascular Research · doi:10.2174/1567202611666140408104831 · Cited by 61

Catalytic mTOR inhibitors can overcome intrinsic and acquired resistance to allosteric mTOR inhibitors

Hassan, B., Akçakanat, A., Sangai, T., Evans, K. W., Adkins, F. C., Eterovic, A. K., Zhao, H., Chen, K., Chen, H., Do, K.-A., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2337 · Cited by 63

Circumventing cellular control of PP2A by methylation promotes transformation in an Akt-dependent manner

Jackson, J. B., & Pallas, D. C. (2012) · Neoplasia · doi:10.1593/neo.12768 · Cited by 60

LPS/TLR4 Pathways in Breast Cancer: Insights into Cell Signalling

Afroz, R., Tanvir, E. M., Tania, M., Fu, J., Kamal, M. A., & Khan, M. A. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210811145043 · Cited by 59

Activation of AMP-Activated Protein Kinase by 5-Aminoimidazole-4-Carboxamide-1-β-D-Ribonucleoside Prevents Leucine-Stimulated Protein Synthesis in Rat Skeletal Muscle

Pruznak, A. M., Kazi, A. A., Frost, R. A., Vary, T. C., & Lang, C. H. (2008) · Journal of Nutrition · doi:10.1093/jn/138.10.1887 · Cited by 58

Leucine Promotes Proliferation and Differentiation of Primary Preterm Rat Satellite Cells in Part through mTORC1 Signaling Pathway

Dai, J.-M., Yu, M., Shen, Z., Guo, C., Zhuang, S., & Qiu, X.-S. (2015) · Nutrients · doi:10.3390/nu7053387 · Cited by 56

Surviving hypoxia by modulation of mRNA translation rate

Fähling, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00875.x · Cited by 54

Effects of Salidroside on Cobalt Chloride-Induced Hypoxia Damage and mTOR Signaling Repression in PC12 Cells

Zhong, X., Lin, R., Li, Z., Mao, J., & Chen, L. (2014) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b14-00100 · Cited by 54

Neuroprotective levels of IGF-1 exacerbate epileptogenesis after brain injury

Song, Y. N., Pimentel, C., Walters, K., Boller, L., Ghiasvand, S., Liu, J., Staley, K. J., & Berdichevsky, Y. (2016) · Scientific Reports · doi:10.1038/srep32095 · Cited by 54

AKT overactivation can suppress DNA repair via p70S6 kinase-dependent downregulation of MRE11

Piscitello, D., Varshney, D., Lilla, S., Vizioli, M. G., Reid, C., Gorbunova, V. A., Seluanov, A., Gillespie, D. A., & Adams, P. D. (2017) · Oncogene · doi:10.1038/onc.2017.340 · Cited by 51

Extracellular vesicles impose quiescence on residual hematopoietic stem cells in the leukemic niche

Abdelhamed, S., Butler, J. T., Doron, B., Halse, A., Nemecek, E. R., Wilmarth, P. A., Marks, D. L., Chang, B. H., Horton, T. M., & Kurre, P. (2019) · EMBO Reports · doi:10.15252/embr.201847546 · Cited by 53

Regulation of mRNA Translation as a Conserved Mechanism of Longevity Control

Mehta, R., Chandler-Brown, D., Ramos, F. J., Shamieh, L. S., & Kaeberlein, M. (2010) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4419-7002-2_2 · Cited by 44

Mammalian Target of Rapamycin (mTOR) Induces Proliferation and De-Differentiation Responses to Three Coordinate Pathophysiologic Stimuli (Mechanical Strain, Hypoxia, and Extracellular Matrix Remodeling) in Rat Bladder Smooth Muscle

AITKEN, K. J., Tölg, C., Panchal, T., Leslie, B., Yu, J., Elkelini, M. S., Sabha, N., Tse, D., Lorenzo, A. J., HASSOUNA, M. M., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2010.080834 · Cited by 49

Roles of PI3K/AKT/PTEN Pathway as a Target for Pharmaceutical Therapy

Matsuda, S., Nakanishi, A., Wada, Y., & Kitagishi, Y. (2013) · The Open Medicinal Chemistry Journal · doi:10.2174/1874104501307010023 · Cited by 49

Inflammatory NF-κB activation promotes hepatic apolipoprotein B100 secretion: evidence for a link between hepatic inflammation and lipoprotein production

Tsai, J., Zhang, R., Qiu, W., Su, Q., Naples, M., & Adeli, K. (2009) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90540.2008 · Cited by 49

Chemical Inhibitors and microRNAs (miRNA) Targeting the Mammalian Target of Rapamycin (mTOR) Pathway: Potential for Novel Anticancer Therapeutics

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Initiation and elongation steps of mRNA translation are involved in the increase in milk protein yield caused by growth hormone administration during lactation

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Valproic acid attenuates skeletal muscle wasting by inhibiting C/EBPβ-regulated atrogin1 expression in cancer cachexia

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Activation of mTOR signaling pathway associated with adverse prognostic factors of epithelial ovarian cancer

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The rationale of targeting mammalian target of rapamycin for ischemic stroke

Chong, Z. Z., Yao, Q., & Li, H. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.03.017 · Cited by 47

Inhibitors of Translation Initiation as Cancer Therapeutics

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Molecular target therapies in endometrial cancer: From the basic research to the clinic

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Extremely low-volume, high-intensity interval training improves exercise capacity and increases mitochondrial protein content in human skeletal muscle

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Translational control by oncogenic signaling pathways

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Impairing the production of ribosomal RNA activates mammalian target of rapamycin complex 1 signalling and downstream translation factors

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mTOR-dependent proliferation defect in human ES-derived neural stem cells affected by Myotonic Dystrophy Type1

Denis, J. A., Gauthier, M., Rachdi, L., Aubert, S., Giraud-Triboult, K., Poydenot, P., Benchoua, A., Champon, B., Maury, Y., Baldeschi, C., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.116285 · Cited by 45

Microcystin-LR promotes proliferation by activating Akt/S6K1 pathway and disordering apoptosis and cell cycle associated proteins phosphorylation in HL7702 cells

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Quantitative Nuclear Proteomics Identifies mTOR Regulation of DNA Damage Response

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Exploring the mTOR Signalling Pathway and Its Inhibitory Scope in Cancer

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Management Options in Triple-Negative Breast Cancer

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Integrative Brain Transcriptome Analysis Reveals Region-Specific and Broad Molecular Changes in Shank3-Overexpressing Mice

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Regulation of ribosomal protein S6 kinases by ubiquitination

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mTOR-Dependent Regulation of Ribosomal Gene Transcription Requires S6K1 and Is Mediated by Phosphorylation of the Carboxy-Terminal Activation Domain of the Nucleolar Transcription Factor UBF†

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THE mTOR SIGNALING PATHWAY AND THE REGULATION OF CELL GROWTH

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

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Ribosomal Protein S6 and S6 Kinases

Pende, M., & Treins, C. (2014) · Springer eBooks · doi:10.1007/978-94-017-9078-9_16

Ribosomal S6 Kinase Signaling and the Control of Translation

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