The nuts and bolts of AGC protein kinases

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 · see citing works

Mechanism by Which Fatty Acids Inhibit Insulin Activation of Insulin Receptor Substrate-1 (IRS-1)-associated Phosphatidylinositol 3-Kinase Activity in Muscle

Yu, C., Chen, Y., Cline, G. W., Zhang, D., Zong, H., Wang, Y., Bergeron, R., Kim, J. K., Cushman, S. W., Cooney, G. J., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200958200 · Cited by 1,561 · see citing works

Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons

Frey, U., Huang, Y.-Y., & Kandel, E. R. (1993) · Science · doi:10.1126/science.8389057 · Cited by 1,218 · see citing works

Inflammatory mechanisms in the regulation of insulin resistance

Tilg, H., & Moschen, A. R. (2008) · Molecular Medicine · doi:10.2119/2007-00119.tilg · Cited by 779 · see citing works

The RSK family of kinases: emerging roles in cellular signalling

Anjum, R., & Blenis, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2509 · Cited by 777 · see citing works

PKC-θ knockout mice are protected from fat-induced insulin resistance

Kim, J. K., Fillmore, J. J., Sunshine, M. J., Albrecht, B., Higashimori, T., Kim, D.-W., Liu, Z.-X., Soos, T. J., Cline, G. W., O’Brien, W. R., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200422230 · Cited by 500 · see citing works

The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation

Mendoza, M. C., Er, E. E., & Blenis, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.006 · Cited by 1,817 · see citing works

Mapping the Hallmarks of Lung Adenocarcinoma with Massively Parallel Sequencing

Imielinski, M., Berger, A. H., Hammerman, P. S., Hernandez, B., Pugh, T. J., Hodis, E., Cho, J., Suh, J., Capelletti, M., Sivachenko, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.08.029 · Cited by 1,789 · see citing works

Mechanisms of Hippo pathway regulation

Meng, Z., Moroishi, T., & Guan, K.-L. (2016) · Genes & Development · doi:10.1101/gad.274027.115 · Cited by 1,667 · 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

Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2.

Copps, K. D., & White, M. F. (2012) · Diabetologia · doi:10.1007/s00125-012-2644-8 · Cited by 1,017 · see citing works

Redox regulation of FoxO transcription factors

Klotz, L.-O., Sánchez-Ramos, C., Prieto-Arroyo, I., Urbánek, P., Steinbrenner, H., & Monsalve, M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.019 · Cited by 747 · see citing works

An atlas of substrate specificities for the human serine/threonine kinome

Johnson, J. L., Yaron, T. M., Huntsman, E. M., Kerelsky, A., Song, J., Regev, A., Lin, T.-Y., Liberatore, K., Cizin, D. M., Cohen, B. M., et al. (2023) · Nature · doi:10.1038/s41586-022-05575-3 · Cited by 728 · see citing works

The metabolic footprint of aging in mice

Houtkooper, R. H., Argmann, C., Houten, S. M., Cantó, C., Jeninga, E. H., Andreux, P. A., Thomas, C., Doenlen, R., Schoonjans, K., & Auwerx, J. (2011) · Scientific Reports · doi:10.1038/srep00134 · Cited by 528 · see citing works

Signalling by insulin and IGF receptors: supporting acts and new players

Siddle, K. (2011) · Journal of Molecular Endocrinology · doi:10.1530/jme-11-0022 · Cited by 456 · 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

Rapid depot-specific activation of adipocyte precursor cells at the onset of obesity

Jeffery, E., Church, C. D., Holtrup, B., Colman, L., & Rodeheffer, M. S. (2015) · Nature Cell Biology · doi:10.1038/ncb3122 · Cited by 404 · see citing works

Selective requirement of PI3K/PDK1 signaling for Kras oncogene-driven pancreatic cell plasticity and cancer

Eser, S., Reiff, N., Messer, M., Seidler, B., Gottschalk, K., Dobler, M., Hieber, M., Arbeiter, A., Klein, S., Kong, B., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.01.023 · Cited by 360 · see citing works

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works

Structural Basis for Activation and Inhibition of Class I Phosphoinositide 3-Kinases

Vadas, O., Burke, J. E., Zhang, X., Berndt, A., & Williams, R. L. (2011) · Science Signaling · doi:10.1126/scisignal.2002165 · Cited by 299 · see citing works

Regulation of AKT Phosphorylation at Ser473 and Thr308 by Endoplasmic Reticulum Stress Modulates Substrate Specificity in a Severity Dependent Manner

Yung, H. W., Charnock-Jones, D. S., & Burton, G. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017894 · Cited by 158 · 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

G-protein coupled receptor, PI3K and Rho signaling pathways regulate the cascades of Tau and amyloid-β in Alzheimer’s disease

Desale, S. E., Chidambaram, H., & Chinnathambi, S. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00036-1 · Cited by 99 · see citing works

Multiple aberrant hormone receptors in Cushing’s syndrome

Ghorayeb, N. E., Bourdeau, I., & Lacroix, A. (2015) · European Journal of Endocrinology · doi:10.1530/eje-15-0200 · Cited by 90 · see citing works

Eccentric contractions increase the phosphorylation of tuberous sclerosis complex‐2 (TSC2) and alter the targeting of TSC2 and the mechanistic target of rapamycin to the lysosome

Jacobs, B. L., You, J., Frey, J. W., Goodman, C. A., Gundermann, D. M., & Hornberger, T. A. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.256339 · Cited by 91 · see citing works

Rho-kinase as a target for cancer therapy and its immunotherapeutic potential

Kim, S., Kim, S. A., Han, J., & Kim, I.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312916 · Cited by 88 · see citing works

TOR kinase complexes and cell migration

Liu, L., & Parent, C. A. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102090 · Cited by 87 · see citing works

Genetic dissection of sodium and potassium transport along the aldosterone‐sensitive distal nephron: Importance in the control of blood pressure and hypertension

Rossier, B. C., Staub, O., & Hummler, E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.013 · Cited by 73 · see citing works

Mammalian target of rapamycin complex 2 regulates muscle glucose uptake during exercise in mice

Kleinert, M., Parker, B. L., Fritzen, A. M., Knudsen, J. R., Jensen, T. E., Kjøbsted, R., Sylow, L., Ruegg, M., James, D. E., & Richter, E. A. (2017) · The Journal of Physiology · doi:10.1113/jp274203 · Cited by 59 · see citing works

The MLL3/4 H3K4 methyltransferase complex in establishing an active enhancer landscape

Wang, L.-H., Aberin, M. A. E., Wu, S., & Wang, S.-P. (2021) · Biochemical Society Transactions · doi:10.1042/bst20191164 · Cited by 53 · see citing works

Phosphorylation of Akt at the C-terminal tail triggers Akt Activation

Liu, P., Wang, Z., & Wei, W. (2014) · Cell Cycle · doi:10.4161/cc.29584 · Cited by 49 · see citing works

Single Copies of Mutant <i>KRAS</i> and Mutant <i>PIK3CA</i> Cooperate in Immortalized Human Epithelial Cells to Induce Tumor Formation

Wang, G. M., Wong, H. Y., Konishi, H., Blair, B. G., Abukhdeir, A. M., Gustin, J. P., Rosen, D. M., Denmeade, S. R., Rasheed, Z., Matsui, W., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-1578 · Cited by 39 · see citing works

PRKX, a Novel cAMP-Dependent Protein Kinase Member, Plays an Important Role in Development: PRKX P<scp>LAYS</scp><scp>AN</scp>I<scp>MPORTANT</scp>R<scp>OLE</scp><scp>IN</scp>D<scp>EVELOPMENT</scp>

Huang, S., Li, Q., Alberts, I., & Li, X. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25304 · Cited by 29 · see citing works

Presence and utility of intrinsically disordered regions in kinases

Kathiriya, J. J., Pathak, R. R., Clayman, E., Xue, B., Uversky, V. N., & Davé, V. (2014) · Molecular BioSystems · doi:10.1039/c4mb00224e · Cited by 30 · see citing works

Inhibition of Microglial GSK3β Activity Is Common to Different Kinds of Antidepressants: A Proposal for an In Vitro Screen to Detect Novel Antidepressant Principles

Kalkman, H. O. (2023) · Biomedicines · doi:10.3390/biomedicines11030806 · Cited by 18 · see citing works

Serum/glucocorticoid regulated kinase 1 (SGK1) in neurological disorders: pain or gain

Howard, P. G., Zou, P., Zhang, Y., Huang, F., Tesic, V., Wu, C. Y.-C., & Lee, R. H.-C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114973 · Cited by 13 · see citing works

The comprehensive SARS-CoV-2 ‘hijackome’ knowledge base

Huuskonen, S., Liu, X., Pöhner, I., Redchuk, T., Salokas, K., Lundberg, R., Maljanen, S., Belik, M., Reinholm, A., Kolehmainen, P., et al. (2024) · Cell Discovery · doi:10.1038/s41421-024-00748-y · Cited by 12 · see citing works

Computational insights into the active structure of SGK1 and its implication for ligand design

Akhoon, B. A., Gandhi, N. S., & Pandey, R. (2019) · Biochimie · doi:10.1016/j.biochi.2019.07.007 · Cited by 9 · see citing works

Behavioral effects of SGK1 knockout in VTA and dopamine neurons

Doyle, M. A., Stark, A. R., Fejes-Tóth, G., Náray-Fejes-Tóth, A., & Mazei-Robison, M. S. (2020) · Scientific Reports · doi:10.1038/s41598-020-71681-9 · Cited by 9 · see citing works