The Phosphoinositide 3-Kinase Pathway

PHOSPHOINOSITIDE KINASES

Fruman, D. A., Meyers, R. E., & Cantley, L. C. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.481 · Cited by 1,382

Transcription-dependent and -independent control of neuronal survival by the PI3K–Akt signaling pathway

Brunet, A., Datta, S. R., & Greenberg, M. E. (2001) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00211-7 · Cited by 1,208

PKB/Akt

Lawlor, M. A., & Alessi, D. R. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.16.2903 · Cited by 1,068

Regulation of C. elegans Life-Span by Insulinlike Signaling in the Nervous System

Wolkow, C. A., Kimura, K. D., Lee, M. S., & Ruvkun, G. (2000) · Science · doi:10.1126/science.290.5489.147 · Cited by 681

PTEN: a tumour suppressor that functions as a phospholipid phosphatase

Maehama, T. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01519-6 · Cited by 599

Constitutive and inducible Akt activity promotes resistance to chemotherapy, trastuzumab, or tamoxifen in breast cancer cells.

Clark, A. S., West, K. A., Streicher, S. A., & Dennis, P. A. (2002) · PubMed · Cited by 589

The lipid phosphatase SHIP2 controls insulin sensitivity

Clément, S., Krause, U., Desmedt, F., Tanti, J., Behrends, J., Pesesse, X., Sasaki, T., Penninger, J. M., Doherty, M., Malaisse, W. J., et al. (2001) · Nature · doi:10.1038/35051094 · Cited by 377

Identification of CISK, a new member of the SGK kinase family that promotes IL-3-dependent survival

Liu, D., Xiao-hong, Y., & Songyang, Z. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00733-8 · Cited by 135

ROS function in redox signaling and oxidative stress

Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931

Cancer genes and the pathways they control

Vogelstein, B., & Kinzler, K. W. (2004) · Nature Medicine · doi:10.1038/nm1087 · Cited by 4,346

Mitochondrial membrane permeabilization in cell death

Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598

Mechanisms of type-I- and type-II-interferon-mediated signalling

Platanias, L. C. (2005) · Nature reviews. Immunology · doi:10.1038/nri1604 · Cited by 3,631

The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism

Engelman, J. A., Luo, J., & Cantley, L. C. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1879 · Cited by 3,330

Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation

Lunt, S. Y., & Vander Heiden, M. G. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154237 · Cited by 3,057

Routes and mechanisms of extracellular vesicle uptake

Mulcahy, L. A., Pink, R. C., & Carter, D. R. F. (2014) · Journal of Extracellular Vesicles · doi:10.3402/jev.v3.24641 · Cited by 2,832

Next Generation of Fluorine-Containing Pharmaceuticals, Compounds Currently in Phase II–III Clinical Trials of Major Pharmaceutical Companies: New Structural Trends and Therapeutic Areas

Zhou, Y., Wang, J., Gu, Z., Wang, S., Zhu, W., Aceña, J. L., Soloshonok, V. A., Izawa, K., & Liu, H. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00392 · Cited by 2,843

Phosphoinositides in cell regulation and membrane dynamics

Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790

Targeting PI3K signalling in cancer: opportunities, challenges and limitations

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

Heme Oxygenase-1/Carbon Monoxide: From Basic Science to Therapeutic Applications

Ryter, S. W., Alam, J., & Choi, A. M. K. (2006) · Physiological Reviews · doi:10.1152/physrev.00011.2005 · Cited by 2,342

The STATs of cancer — new molecular targets come of age

Yu, H., & Jove, R. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1275 · Cited by 2,278

Neurotrophin-regulated signalling pathways

Reichardt, L. F. (2006) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1894 · Cited by 2,195

Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling

Wang, Y., Branicky, R. S., Noë, A., & Hekimi, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201708007 · Cited by 2,284

PI3K/AKT/mTOR signaling transduction pathway and targeted therapies in cancer

Glaviano, A., Foo, A. S. C., Lam, H. Y., Yap, K. C. H., Jacot, W., Jones, R. H., Eng, H., Nair, M. G., Makvandi, P., Geoerger, B., et al. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01827-6 · Cited by 2,138

Function and regulation of CREB family transcription factors in the nervous system

Lonze, B. E., & Ginty, D. D. (2002) · Neuron · doi:10.1016/s0896-6273(02)00828-0 · Cited by 2,127

Targeting PI3K/Akt signal transduction for cancer therapy

He, Y., Sun, M., Zhang, G. G., Yang, J., Chen, K. S., Xu, W. W., & Li, B. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00828-5 · Cited by 2,045

The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors.

Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964

PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients

Nagata, Y., Lan, K.-H., Zhou, X., Tan, M., Esteva, F. J., Sahin, A. A., Klos, K. S., Li, P., Monia, B. P., Nguyen, N. T., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.06.022 · Cited by 1,858

Regulation of cardiac hypertrophy by intracellular signalling pathways

Heineke, J., & Molkentin, J. D. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1983 · Cited by 1,890

PI3K pathway alterations in cancer: variations on a theme

Yuan, T. L., & Cantley, L. C. (2008) · Oncogene · doi:10.1038/onc.2008.245 · Cited by 1,845

Regulation of Mammalian Autophagy in Physiology and Pathophysiology

Ravikumar, B., Sarkar, S., Davies, J. E., Futter, M., García-Arencibia, M., Green-Thompson, Z. W., Jiménez-Sánchez, M., Korolchuk, V. I., Lichtenberg, M., Luo, S., et al. (2010) · Physiological Reviews · doi:10.1152/physrev.00030.2009 · Cited by 1,789

Molecular mechanisms of drug resistance

Longley, D., & Johnston, P. (2005) · The Journal of Pathology · doi:10.1002/path.1706 · Cited by 1,726

Signal Transduction by Vascular Endothelial Growth Factor ReceptorsPreprint

Koch, S., Tugues, S., Li, X., Gualandi, L., & Claesson, L. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1042/bj20110301 · Cited by 1,710

Reprogramming of fatty acid metabolism in cancer

Koundouros, N., & Poulogiannis, G. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0650-z · Cited by 1,669

Genetics and biology of pancreatic ductal adenocarcinomaPreprint

Hezel, A. F., Kimmelman, A. C., Stanger, B. Z., Bardeesy, N. M., & DePinho, R. A. (2006) · Genes & Development · doi:10.1101/gad.1415606 · Cited by 1,611

Epidermal growth factor receptor: Mechanisms of activation and signalling

Jorissen, R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00098-8 · Cited by 1,565

NF-κB activation by reactive oxygen species: Fifteen years later

Gloire, G., Legrand-Poels, S., & Piette, J. G. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.04.011 · Cited by 1,561

Cardiac Hypertrophy: The Good, the Bad, and the Ugly

Frey, N., & Olson, E. N. (2003) · Annual Review of Physiology · doi:10.1146/annurev.physiol.65.092101.142243 · Cited by 1,480

Membrane recognition by phospholipid-binding domains

Lemmon, M. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2328 · Cited by 1,419

Molecular determinants of the response of glioblastomas to EGFR kinase inhibitors

Mellinghoff, I. K., Wang, M. Y., Vivanco, I., Haas-Kogan, D. A., Zhu, S., Dia, E. Q., Lu, K. V., Yoshimoto, K., Huang, J. H. Y., Chute, D. J., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa051918 · Cited by 1,442

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

Targeting Apoptosis Pathways in Cancer Therapy

Ghobrial, I. M., Witzig, T. E., & Adjei, A. A. (2005) · CA A Cancer Journal for Clinicians · doi:10.3322/canjclin.55.3.178 · Cited by 1,369

FOXO transcription factors at the interface between longevity and tumor suppression

Greer, E. L., & Brunet, A. (2005) · Oncogene · doi:10.1038/sj.onc.1209086 · Cited by 1,340

A transforming mutation in the pleckstrin homology domain of AKT1 in cancer

Carpten, J. D., Faber, A. L., Horn, C. L., Donoho, G. P., Briggs, S., Robbins, C. M., Hostetter, G. H., Boguslawski, S. J., Moses, T. Y., Savage, S., et al. (2007) · Nature · doi:10.1038/nature05933 · Cited by 1,322

Targeting the PI3K-Akt pathway in human cancer

Luo, J., Manning, B. D., & Cantley, L. C. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00248-4 · Cited by 1,290

Lipid signalling in disease

Wymann, M. P., & Schneiter, R. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2335 · Cited by 1,314

Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression

Fingar, D. C., & Blenis, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207542 · Cited by 1,264

The PI3K Pathway As Drug Target in Human Cancer

Courtney, K. D., Corcoran, R. B., & Engelman, J. A. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.25.3641 · Cited by 1,268

Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: a target for cancer chemotherapy

Chang, F., Lee, J. T., Navolanic, P. M., Steelman, L. S., Shelton, J. G., Blalock, W. L., Franklin, R. A., & McCubrey, J. A. (2003) · Leukemia · doi:10.1038/sj.leu.2402824 · Cited by 1,176

Novel anticancer targets: revisiting ERBB2 and discovering ERBB3

Baselga, J. M., & Swain, S. M. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2656 · Cited by 1,170

Dual Role of 3-Methyladenine in Modulation of Autophagy via Different Temporal Patterns of Inhibition on Class I and III Phosphoinositide 3-Kinase

Wu, Y.-T., Tan, H.-L., Shui, G., Bauvy, C., Huang, Q., Wenk, M. R., Ong, C.-N., Codogno, P., & Shen, H.-M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.080796 · Cited by 1,127

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

Metabolic regulation of cell growth and proliferation

Zhu, J., & Thompson, C. B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0123-5 · Cited by 1,154

Role of Mitochondrial Dysfunction in Insulin Resistance

Kim, J.-A., Wei, Y., & Sowers, J. R. (2008) · Circulation Research · doi:10.1161/circresaha.107.165472 · Cited by 1,103

Toll-like receptor–mediated cytokine production is differentially regulated by glycogen synthase kinase 3

Martin, M., Rehani, K., Jope, R. S., & Michalek, S. M. (2005) · Nature Immunology · doi:10.1038/ni1221 · Cited by 1,099

Principles of Tumor Suppression

Sherr, C. J. (2004) · Cell · doi:10.1016/s0092-8674(03)01075-4 · Cited by 1,028

Signaling cross-talk between TGF-β/BMP and other pathways

Guo, X., & Wang, X. (2008) · Cell Research · doi:10.1038/cr.2008.302 · Cited by 1,077

Vascular endothelial growth factor receptor-2: Structure, function, intracellular signalling and therapeutic inhibition

Holmes, K., Roberts, O. L., Thomas, A. M., & Cross, M. J. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.05.013 · Cited by 1,053

Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes

Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011

Autophagy: dual roles in life and death?

Baehrecke, E. H. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1666 · Cited by 986

Notch signalling regulates stem cell numbers in vitro and in vivo

Androutsellis‐Theotokis, A., Leker, R. R., Soldner, F., Hoeppner, D. J., Ravin, R., Poser, S., Rueger, M. A., Bae, S., Kittappa, R., & McKay, R. D. G. (2006) · Nature · doi:10.1038/nature04940 · Cited by 963

Coactivation of receptor tyrosine kinases affects the response of tumor cells to targeted therapies

Stommel, J. M., Kimmelman, A. C., Ying, H., Nabioullin, R., Ponugoti, A. H., Wiedemeyer, R., Stegh, A. H., Bradner, J. E., Ligon, K. L., Brennan, C., et al. (2007) · Science · doi:10.1126/science.1142946 · Cited by 938

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

Molecular distinction between physiological and pathological cardiac hypertrophy: Experimental findings and therapeutic strategies

Bernardo, B. C., Weeks, K. L., Pretorius, L., & McMullen, J. R. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.04.005 · Cited by 920

The PTEN–PI3K pathway: of feedbacks and cross-talks

Carracedo, A., & Pandolfi, P. P. (2008) · Oncogene · doi:10.1038/onc.2008.247 · Cited by 908

Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling

Koivusalo, M., Welch, C. M., Hayashi, H., Scott, C. C., Kim, M., Alexander, T. R., Touret, N., Hahn, K. M., & Grinstein, S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200908086 · Cited by 878

Post-translational modifications in signal integration

Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876

Cardiovascular Actions of Insulin

Muniyappa, R., Montagnani, M., Koh, K. K., & Quon, M. J. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0006 · Cited by 888

Plasma membrane phosphoinositide organization by protein electrostatics

McLaughlin, S., & Murray, D. (2005) · Nature · doi:10.1038/nature04398 · Cited by 868

Oocyte-Specific Deletion of Pten Causes Premature Activation of the Primordial Follicle Pool

Reddy, P., Liu, L., Adhikari, D., Jagarlamudi, K., Singareddy, R., Shen, Y., Du, C., Tang, W., Hämäläinen, T. M., Peng, S. L., et al. (2008) · Science · doi:10.1126/science.1152257 · Cited by 874

Hypertrophy of the Heart

Frey, N., Katus, H. A., Olson, E. N., & Hill, J. A. (2004) · Circulation · doi:10.1161/01.cir.0000120390.68287.bb · Cited by 859

Activation of AKT Kinases in Cancer: Implications for Therapeutic Targeting

Bellacosa, A., Kumar, C. C., Cristofano, A. D., & Testa, J. R. (2005) · Advances in cancer research · doi:10.1016/s0065-230x(05)94002-5 · Cited by 844

Apoptosis and melanoma chemoresistance

Soengas, M. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1206454 · Cited by 836

PDK1, the master regulator of AGC kinase signal transduction

Mora, A., Komander, D., van Aalten, D. M. F., & Alessi, D. R. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2003.12.022 · Cited by 818

Mitochondrial reactive oxygen species and cancer

Sullivan, L. B., & Chandel, N. S. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-17 · Cited by 823

Oncogenic PI3K deregulates transcription and translation

Bader, A. G., Kang, S., Zhao, L., & Vogt, P. K. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1753 · Cited by 807

NVP-BEZ235, a Dual PI3K/mTOR Inhibitor, Prevents PI3K Signaling and Inhibits the Growth of Cancer Cells with Activating PI3K Mutations

Serra, V., Markman, B., Scaltriti, M., Eichhorn, P. J. A., Valero, V., Guzman, M., Botero, M. L., Llonch, E., Atzori, F., Di Cosimo, S., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1385 · Cited by 787

Attacking the PI3K/Akt/mTOR signaling pathway for targeted therapeutic treatment in human cancer

Yu, L., Wei, J., & Liu, P. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.06.019 · Cited by 818

PI 3-kinase, Akt and cell survival

Downward, J. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2004.01.002 · Cited by 791

Molecular targets for cancer therapy in the PI3K/AKT/mTOR pathway

Polivka, J., & Janku, F. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.004 · Cited by 765

RAS Interaction with PI3K: More Than Just Another Effector Pathway

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

The Identification of 2-(1 H -Indazol-4-yl)-6-(4-methanesulfonyl-piperazin-1-ylmethyl)-4-morpholin-4-yl-thieno[3,2- d ]pyrimidine (GDC-0941) as a Potent, Selective, Orally Bioavailable Inhibitor of Class I PI3 Kinase for the Treatment of Cancer

Folkes, A. J., Ahmadi, K., ALDERTON, W. K., Alix, S., Baker, S. J., Box, G., Chuckowree, I., Clarke, P. A., Depledge, P., Eccles, S. A., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800295d · Cited by 756

Ubiquitination regulates PTEN nuclear import and tumor suppression

Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748

Ca2+ signalling checkpoints in cancer: remodelling Ca2+ for cancer cell proliferation and survival

Roderick, H. L., & Cook, S. J. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2374 · Cited by 752

Activation of Platelet Function Through G Protein–Coupled Receptors

Offermanns, S. (2006) · Circulation Research · doi:10.1161/01.res.0000251742.71301.16 · Cited by 725

Regulation of glucose homeostasis by glucocorticoids

Kuo, T., McQueen, A., Chen, T.-C., & Wang, J.-C. (2015) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4939-2895-8_5 · Cited by 723

Mammalian target of rapamycin: a central node of complex signaling cascades.

Dobashi, Y., Watanabe, Y., Miwa, C., Suzuki, S., & Koyama, S. (2011) · PubMed Central · Cited by 721

Phase I, Dose-Escalation Study of BKM120, an Oral Pan-Class I PI3K Inhibitor, in Patients With Advanced Solid Tumors

Bendell, J. C., Rodon, J. A., Burris, H. A., de Jonge, M. J. A., Verweij, J., Birle, D. C., Demanse, D., Buck, S. S. D., Ru, Q. C., Peters, M., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2011.36.1360 · Cited by 703

JAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis

Steelman, L. S., Pohnert, S. C., Shelton, J. G., Franklin, R. A., Bertrand, F. E., & McCubrey, J. A. (2004) · Leukemia · doi:10.1038/sj.leu.2403241 · Cited by 705

The E3 Ligase TRAF6 Regulates Akt Ubiquitination and Activation

Yang, W., Wang, J., Chan, C., Lee, S.-W., Campos, A. D., Lamothe, B., Hur, L., Grabiner, B. C., Lin, X., Darnay, B. G., et al. (2009) · Science · doi:10.1126/science.1175065 · Cited by 669

The PI3K-AKT-mTOR Pathway and Prostate Cancer: At the Crossroads of AR, MAPK, and WNT Signaling

Shorning, B. Y., Dass, M. S., Smalley, M. J., & Pearson, H. B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124507 · Cited by 652

Diffuse glioma growth: a guerilla war

Claes, A., Idema, A. J. S., & Wesseling, P. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0293-7 · Cited by 648

Thromboinflammation: challenges of therapeutically targeting coagulation and other host defense mechanisms

Jackson, S. P., Darbousset, R., & Schoenwaelder, S. M. (2019) · Blood · doi:10.1182/blood-2018-11-882993 · Cited by 644

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

Yang, X., Ongusaha, P. P., Miles, P. D. G., Havstad, J. C., Zhang, F., So, W. V., Kudlow, J. E., Michell, R. H., Olefsky, J. M., Field, S. J., et al. (2008) · Nature · doi:10.1038/nature06668 · Cited by 639

Redox regulation of PI 3‐kinase signalling via inactivation of PTEN

Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 631

Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathwayPreprint

Puig, Ó., Marr, M. T., Ruhf, M.-L., & Tjian, R. (2003) · Genes & Development · doi:10.1101/gad.1098703 · Cited by 628

Insulin resistance and cancer risk: An overview of the pathogenetic mechanisms

Arcidiacono, B., Iiritano, S., Nocera, A., Possidente, K., Nevolo, M. T., Ventura, V., Foti, D., Chiefari, E., & Brunetti, A. (2012) · Experimental Diabetes Research · doi:10.1155/2012/789174 · Cited by 606

The Two Faces of Reactive Oxygen Species in Cancer

Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602

Hippocampal Neuronal Polarity Specified by Spatially Localized mPar3/mPar6 and PI 3-Kinase Activity

Shi, S.-H., Jan, L. Y., & Jan, Y.-N. (2003) · Cell · doi:10.1016/s0092-8674(02)01249-7 · Cited by 600

Phosphorylation of IRS proteins, insulin action, and insulin resistance

Boura-Halfon, S., & Zick, Y. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90437.2008 · Cited by 598

Class I PI3K in oncogenic cellular transformation

Zhao, L., & Vogt, P. K. (2008) · Oncogene · doi:10.1038/onc.2008.244 · Cited by 612

The Drosophila Forkhead transcription factor FOXO mediates the reduction in cell number associated with reduced insulin signaling

Jünger, M. A., Rintelen, F., Stocker, H., Wasserman, J. D., Végh, M., Radimerski, T., Greenberg, M. E., & Hafen, E. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-20 · Cited by 595

The PI3K/AKT/mTOR pathway in breast cancer: targets, trials and biomarkers

Paplomata, E., & O'Regan, R. M. (2014) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834014530023 · Cited by 610

The deaf and the dumb: the biology of ErbB-2 and ErbB-3

Citri, A. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00101-5 · Cited by 603

Convergent loss of PTEN leads to clinical resistance to a PI(3)Kα inhibitor

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