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

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302

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

Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain

Lemmon, M. A., Ferguson, K. M., O'Brien, R., Sigler, P. B., & Schlessinger, J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10472 · Cited by 566

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

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

Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689

AKT/PKB Signaling: Navigating the Network

Manning, B. D., & Toker, A. (2017) · Cell · doi:10.1016/j.cell.2017.04.001 · Cited by 3,772

Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation

Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591

Mechanisms of Insulin Action and Insulin Resistance

Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028

Defining the role of mTOR in cancer

Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833

Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN

Stambolic, V., Suzuki, A., de la Pompa, J. L., Brothers, G. M., Mirtsos, C., Sasaki, T., Ruland, J., Penninger, J. M., Siderovski, D. P., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81780-8 · Cited by 2,551

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

The PI3K–AKT network at the interface of oncogenic signalling and cancer metabolism

Hoxhaj, G., & Manning, B. D. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-019-0216-7 · Cited by 2,137

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

Excitotoxicity and stroke: Identifying novel targets for neuroprotection

Lai, T. W., Zhang, S., & Wang, Y. T. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.11.006 · Cited by 1,106

Role of Translocation in the Activation and Function of Protein Kinase B

Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J. C., Frech, M., Cron, P., Cohen, P., Lucocq, J. M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31515 · Cited by 1,051

Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling

SHEPHERD, P. R., WITHERS, D. J., & SIDDLE, K. (1998) · Biochemical Journal · doi:10.1042/bj3330471 · Cited by 953

PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth

Gao, T., Furnari, F., & Newton, A. C. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.008 · Cited by 906

AMP-activated Protein Kinase Suppresses Protein Synthesis in Rat Skeletal Muscle through Down-regulated Mammalian Target of Rapamycin (mTOR) Signaling

Bolster, D. R., Crozier, S. J., Kimball, S. R., & Jefferson, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200171200 · Cited by 851

The two TORCs and Akt

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

Time of feeding and the intrinsic circadian clock drive rhythms in hepatic gene expression.

Vollmers, C., Gill, S., DiTacchio, L., Pulivarthy, S. R., Le, H. D., & Panda, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909591106 · Cited by 765

Roles for Insulin Receptor, PI3-Kinase, and Akt in Insulin-Signaling Pathways Related to Production of Nitric Oxide in Human Vascular Endothelial Cells

Zeng, G., Nystrom, F. H., Ravichandran, L. V., Cong, L.-N., Kirby, M., Mostowski, H., & Quon, M. J. (2000) · Circulation · doi:10.1161/01.cir.101.13.1539 · Cited by 745

AKT/PKB and Other D3 Phosphoinositide-Regulated Kinases: Kinase Activation by Phosphoinositide-Dependent Phosphorylation

Chan, T. O., Rittenhouse, S. E., & Tsichlis, P. N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.965 · Cited by 737

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

FKBP51 Affects Cancer Cell Response to Chemotherapy by Negatively Regulating Akt

Pei, H., Li, L., Fridley, B. L., Jenkins, G. D., Kalari, K. R., Lingle, W., Petersen, G., Lou, Z., & Wang, L. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.07.016 · Cited by 709

Ribosomal S6 Kinase Signaling and the Control of Translation

Dufner, A., & Thomas, G. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4683 · Cited by 676

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

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631

Macrophage binding to receptor VCAM-1 transmits survival signals in breast cancer cells that invade the lungs

Chen, Q., Zhang, X. H.-F., & Massagué, J. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.025 · Cited by 619

Neurorestorative therapies for stroke: underlying mechanisms and translation to the clinic

Zhang, Z. G., & Chopp, M. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70061-4 · Cited by 596

Selective effects of PD-1 on Akt and Ras pathways regulate molecular components of the cell cycle and inhibit T cell proliferation

Patsoukis, N., Brown, J., Petkova, V., Liu, F., Li, L., & Boussiotis, V. A. (2012) · Science Signaling · doi:10.1126/scisignal.2002796 · Cited by 529

Activation of the phosphoinositide 3-kinase-Akt-mammalian target of rapamycin signaling pathway is required for metabotropic glutamate receptor-dependent long-term depression

Hou, L., & Klann, E. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.0995-04.2004 · Cited by 527

Role of Skeletal Muscle in Insulin Resistance and Glucose Uptake

Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive Physiology · doi:10.1002/cphy.c190029 · Cited by 494

Biologic sequelae of interleukin-6 induced PI3-K/Akt signaling in multiple myeloma

Hideshima, T., Nakamura, N., Chauhan, D., & Anderson, K. C. (2001) · Oncogene · doi:10.1038/sj.onc.1204833 · Cited by 478

Regulation of Insulin-Stimulated Glucose Transporter GLUT4 Translocation and Akt Kinase Activity by Ceramide

Summers, S. A., Garza, L. A., Zhou, H., & Birnbaum, M. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5457 · Cited by 475

Selective activation of AMPK‐PGC‐1α or PKB‐TSC2‐mTOR signaling can explain specific adaptive responses to endurance or resistance training‐like electrical muscle stimulation

Atherton, P. J., Babraj, J. A., Smith, K., Singh, J., Rennie, M. J., & Wackerhage, H. (2005) · The FASEB Journal · doi:10.1096/fj.04-2179fje · Cited by 475

TOR signalling and control of cell growth

Thomas, G., & Hall, M. N. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80078-6 · Cited by 462

The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system

Pich, S., Bach, D., Briones, P., Liesa, M., Camps, M., Testar, X., Palacín, M., & Zorzano, A. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi149 · Cited by 455

mTOR Kinase Inhibition Causes Feedback-Dependent Biphasic Regulation of AKT Signaling

Rodrik-Outmezguine, V. S., Chandarlapaty, S., Pagano, N. C., Poulikakos, P. I., Scaltriti, M., Moskatel, E., Baselga, J., Guichard, S., & Rosen, N. (2011) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0085 · Cited by 442

Reversal of diet-induced hepatic steatosis and hepatic insulin resistance by antisense oligonucleotide inhibitors of acetyl-CoA carboxylases 1 and 2

Savage, D. B. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27300 · Cited by 447

The Genetics of Aging

Finch, C. E., & Ruvkun, G. (2001) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.2.1.435 · Cited by 446

Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase

KOBAYASHI, T., DEAK, M., MORRICE, N., & COHEN, P. (1999) · Biochemical Journal · doi:10.1042/bj3440189 · Cited by 405

Expression of CX 3 CR1 chemokine receptors on neurons and their role in neuronal survival

Meucci, O., Fatatis, A., Simen, A. A., & Miller, R. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.090017497 · Cited by 385

Suppression of Diacylglycerol Acyltransferase-2 (DGAT2), but Not DGAT1, with Antisense Oligonucleotides Reverses Diet-induced Hepatic Steatosis and Insulin Resistance

Choi, C. S., Savage, D. B., Kulkarni, A., Yu, X. X., Liu, Z.-X., Morino, K., Kim, S., Distefano, A., Samuel, V. T., Neschen, S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704213200 · Cited by 383

Hydrogen Peroxide Activates Endothelial Nitric-oxide Synthase through Coordinated Phosphorylation and Dephosphorylation via a Phosphoinositide 3-Kinase-dependent Signaling Pathway

Thomas, S. R., Chen, K., & Keaney, J. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109107200 · Cited by 381

Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ

Meier, R., Alessi, D. R., Cron, P., Andjelković, M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30491 · Cited by 378

PI3K/AKT pathway mutations cause a spectrum of brain malformations from megalencephaly to focal cortical dysplasia

Jansen, L. A., Mirzaa, G. M., Ishak, G. E., O'Roak, B. J., Hiatt, J. B., Roden, W. H., Gunter, S. A., Christian, S. L., Collins, S., Adams, C., et al. (2015) · Brain · doi:10.1093/brain/awv045 · Cited by 364

Regulation of Phosphorylation of Thr-308 of Akt, Cell Proliferation, and Survival by the B55α Regulatory Subunit Targeting of the Protein Phosphatase 2A Holoenzyme to Akt

Kuo, Y.-C., Huang, K.-Y., Yang, C.-H., Yang, Y.-S., Lee, W.-Y., & Chiang, C.-W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709585200 · Cited by 367

The Rac1-GEF Tiam1 couples the NMDA receptor to the activity-dependent development of dendritic arbors and spines

Tolias, K. F., Bikoff, J. B., Burette, A., Paradis, S., Harrar, D., Tavazoie, S., Weinberg, R. J., & Greenberg, M. E. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.024 · Cited by 365

mTOR Complex 2 Is Required for the Development of Prostate Cancer Induced by Pten Loss in Mice

Guertin, D. A., Stevens, D. M., Saitoh, M., Kinkel, S., Crosby, K., Sheen, J.-H., Mullholland, D. J., Magnuson, M. A., Wu, H., & Sabatini, D. M. (2009) · Cancer Cell · doi:10.1016/j.ccr.2008.12.017 · Cited by 355

Regulation of Glucose-6-phosphatase Gene Expression by Protein Kinase Bα and the Forkhead Transcription Factor FKHR

Schmoll, D., Walker, K. S., Alessi, D. R., Grempler, R., Burchell, A., Guo, S., Walther, R., & Unterman, T. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003616200 · Cited by 349

Transgenic Mice Overexpressing Glycogen Synthase Kinase 3β: A Putative Model of Hyperactivity and Mania

Prickaerts, J., Moechars, D., Cryns, K., Lenaerts, I., van Craenendonck, H., Goris, I., Daneels, G., Bouwknecht, J. A., & Steckler, T. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5216-05.2006 · Cited by 341

AMP-activated protein kinase (AMPK) signaling in endothelial cells is essential for angiogenesis in response to hypoxic stress

Nagata, D., Mogi, M., & Walsh, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300643200 · Cited by 331

Activation of AMP-activated protein kinase inhibits protein synthesis associated with hypertrophy in the cardiac myocyte

Chan, A. Y. M., Soltys, C.-L. M., Young, M. E., Proud, C. G., & Dyck, J. R. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403528200 · Cited by 331

Continuous fat oxidation in acetyl-CoA carboxylase 2 knockout mice increases total energy expenditure, reduces fat mass, and improves insulin sensitivity

Choi, C. S., Savage, D. B., Abu-Elheiga, L., Liu, Z.-X., Kim, S., Kulkarni, A., Distefano, A., Hwang, Y.-J., Reznick, R. M., Codella, R., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706794104 · Cited by 325

Soluble Aβ Inhibits Specific Signal Transduction Cascades Common to the Insulin Receptor Pathway

Townsend, M., Mehta, T., & Selkoe, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610390200 · Cited by 318

Akt provides the CD28 costimulatory signal for up-regulation of IL-2 and IFN-γ but not TH2 cytokines

Kane, L. P., Andres, P. G., Howland, K. C., Abbas, A. K., & Weiss, A. (2001) · Nature Immunology · doi:10.1038/83144 · Cited by 316

AMPK and Exercise: Glucose Uptake and Insulin Sensitivity

O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295

A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation

Frödin, M., Antal, T. L., Dümmler, B. A., Jensen, C. J., Deak, M., Gammeltoft, S., & Biondi, R. M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf551 · Cited by 275

KLRG1 signaling induces defective Akt (ser473) phosphorylation and proliferative dysfunction of highly differentiated CD8+ T cells

Henson, S. M., Franzese, O., Macaulay, R., Libri, V., Azevedo, R. I., Kiani-Alikhan, S., Plunkett, F. J., Masters, J. E., Jackson, S., Griffiths, S. J., et al. (2009) · Blood · doi:10.1182/blood-2009-01-199588 · Cited by 262

Identification of Host-Targeted Small Molecules That Restrict Intracellular Mycobacterium tuberculosis Growth

Stanley, S. A., Barczak, A. K., Silvis, M. R., Luo, S. S., Sogi, K., Vokes, M., Bray, M.-A., Carpenter, A. E., Moore, C. B., Siddiqi, N., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003946 · Cited by 251

PDK1, one of the missing links in insulin signal transduction?1

Cohen, P., Alessi, D. R., & Cross, D. A. E. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00490-0 · Cited by 246

Activation of AMP kinase enhances sensitivity of muscle glucose transport to insulin

Fisher, J. S., Gao, J., Han, D.-H., Holloszy, J. O., & Nolte, L. A. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2002.282.1.e18 · Cited by 244

RTP801 Is Induced in Parkinson's Disease and Mediates Neuron Death by Inhibiting Akt Phosphorylation/Activation

Malagelada, C., Jin, Z. H., & Greene, L. A. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3928-08.2008 · Cited by 228

Comparative signaling pathways of insulin-like growth factor-1 and brain-derived neurotrophic factor in hippocampal neurons and the role of the PI3 kinase pathway in cell survival

Zheng, W., & Quirion, R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02350.x · Cited by 225

The loss of telomerase activity in highly differentiated CD8+CD28−CD27− T cells is associated with decreased Akt (Ser473) phosphorylation

Plunkett, F. J., Franzese, O., Finney, H. M., Fletcher, J. M., Belaramani, L. L., Salmon, M., Dokal, I., Webster, D., Lawson, A. D. G., & Akbar, A. N. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.12.7710 · Cited by 222

Txnip balances metabolic and growth signaling via PTEN disulfide reduction

Hui, S. T. Y., Andres, A. M., Miller, A. K., Spann, N. J., Potter, D. W., Post, N. M., Chen, A. Z., Sachithanantham, S., Jung, D. Y., Kim, J. K., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800293105 · Cited by 214

Activation of Lipoprotein Lipase by Glucose-dependent Insulinotropic Polypeptide in Adipocytes

Kim, S.-J., Nian, C., & McIntosh, C. H. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609088200 · Cited by 216

Untitled work

(2010) · doi:10.1074/jbc.m110.168039 · Cited by 207

Skeletal Muscle-Selective Knockout of LKB1 Increases Insulin Sensitivity, Improves Glucose Homeostasis, and Decreases TRB3

Koh, H.-J., Arnolds, D. E., Fujii, N., Tran, T. T., Rogers, M. J., Jessen, N., Li, Y., Liew, C. W., Ho, R. C., Hirshman, M. F., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00979-06 · Cited by 202

Untitled work

(2001) · PubMed · Cited by 193

Brain Development and Akt Signaling: the Crossroads of Signaling Pathway and Neurodevelopmental Diseases

Wang, L., Zhou, K., Fu, Z., Yu, D., Huang, H., Zang, X., & Mo, X. (2017) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0872-y · Cited by 172

Mammary gland involution is delayed by activated Akt in transgenic mice

Schwertfeger, K. L., Richert, M. M., & Anderson, S. M. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.6.0663 · Cited by 169

Insulin signaling and glucose transport in insulin resistant human skeletal muscle

Karlsson, H. K. R., & Zierath, J. R. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0030-9 · Cited by 159

The Inositol Phosphatase SHIP Inhibits Akt/PKB Activation in B Cells

Aman, M. J., Lamkin, T. D., Okada, H., Kurosaki, T., & Ravichandran, K. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33922 · Cited by 162

Dysregulation of the IGF‐I/PI3K/AKT/mTOR signaling pathway in autism spectrum disorders

Chen, J., Alberts, I., & Li, X. (2014) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2014.03.006 · Cited by 151

FoxO maintains a genuine muscle stem-cell quiescent state until geriatric age

García-Prat, L., Perdiguero, E., Alonso-Martín, S., Dell’Orso, S., Ravichandran, S., Brooks, S. R., Juan, A. H., Campanario, S., Jiang, K., Hong, X., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00593-7 · Cited by 161

The Croonian Lecture 1998. Identification of a protein kinase cascade of major importance in insulin signal transduction

Cohen, P. (1999) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.1999.0399 · Cited by 158

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

Neuropathological role of PI3K/Akt/mTOR axis in Down syndrome brain

Perluigi, M., Pupo, G., Tramutola, A., Cini, C., Coccia, R., Barone, E., Head, E., Butterfield, D. A., & Di Domenico, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.04.007 · Cited by 155

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

Activation of Endothelial Nitric-oxide Synthase by the p38 MAPK in Response to Black Tea Polyphenols

Anter, E., Thomas, S. R., Schulz, E., Shapira, O. M., Vita, J. A., & Keaney, J. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405547200 · Cited by 142

The pro‐apoptotic kinase Mst1 and its caspase cleavage products are direct inhibitors of Akt1

Cinar, B., Fang, P., Lutchman, M., Di Vizio, D., Adam, R. M., Pavlova, N., Rubin, M. A., Yelick, P. C., & Freeman, M. R. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601872 · Cited by 136

Regulation of PTEN translation by PI3K signaling maintains pathway homeostasis

Mukherjee, R., Vanaja, K. G., Boyer, J. A., Gadal, S., Solomon, H., Chandarlapaty, S., Levchenko, A., & Rosen, N. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.033 · Cited by 135

Protein kinase B activity is required for the effects of insulin on lipid metabolism in adipocytes

Berggreen, C., Gormand, A., Omar, B., Degerman, E., & Göransson, O. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90596.2008 · Cited by 118

Brain-derived neurotrophic factor activation of CaM-kinase kinase via transient receptor potential canonical channels induces the translation and synaptic incorporation of GluA1-containing calcium-permeable AMPA receptors

Fortin, D. A., Srivastava, T., Dwarakanath, D., Pierre, P., Nygaard, S., Derkach, V. A., & Soderling, T. R. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6034-11.2012 · Cited by 120

Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle

Arias, E. B., Kim, J., Funai, K., & Cartee, G. D. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00602.2006 · Cited by 118

Phospholipid-binding protein domains

Bottomley, M. J., Salim, K., & Panayotou, G. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s0005-2760(98)00141-6 · Cited by 118

Acute exercise and physiological insulin induce distinct phosphorylation signatures on TBC1D1 and TBC1D4 proteins in human skeletal muscle

Treebak, J. T., Pehmøller, C., Kristensen, J. M., Kjøbsted, R., Birk, J. B., Schjerling, P., Richter, E. A., Goodyear, L. J., & Wojtaszewski, J. F. P. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2013.266338 · Cited by 113

Muscle glycogen inharmoniously regulates glycogen synthase activity, glucose uptake, and proximal insulin signaling

Jensen, J., Jebens, E., Brennesvik, E. O., Ruzzin, J., Soos, M. A., Engebretsen, E. M. L., O'Rahilly, S., & Whitehead, J. P. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00330.2005 · Cited by 114

Evidence of endoplasmic reticulum stress and protein synthesis inhibition in the placenta of non‐native women at high altitude

Yung, H. W., Cox, M., van Patot, M. T., & Burton, G. J. (2012) · The FASEB Journal · doi:10.1096/fj.11-190082 · Cited by 112

Sall4 regulates cell fate decision in fetal hepatic stem/progenitor cells

Oikawa, T., Kamiya, A., Kakinuma, S., Zeniya, M., Nishinakamura, R., Tajiri, H., & Nakauchi, H. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.11.018 · Cited by 108

Effect of high-intensity exercise on aged mouse brain mitochondria, neurogenesis, and inflammation

E, L., Burns, J. M., & Swerdlow, R. H. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.05.033 · Cited by 106

Clk2 and B56β mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt

Rodgers, J. T., Vogel, R. O., & Puigserver, P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.007 · Cited by 99

Insulin and IGF1 signalling pathways in human astrocytes in vitro and in vivo; characterisation, subcellular localisation and modulation of the receptors

Garwood, C. J., Ratcliffe, L. E., Morgan, S. V., Simpson, J. E., Owens, H., Vazquez-Villaseñor, I., Heath, P. R., Romero, I. A., Ince, P. G., & Wharton, S. B. (2015) · Molecular Brain · doi:10.1186/s13041-015-0138-6 · Cited by 101

Differential Roles of Insulin Receptor Substrates in the Anti-apoptotic Function of Insulin-like Growth Factor-1 and Insulin

Tseng, Y.-H., Ueki, K., Kriauciunas, K. M., & Kahn, C. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202932200 · Cited by 96

The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane

Berndt, N., Yang, H., Trinczek, B., Betzi, S., Zhang, Z., Wu, B., Lawrence, N. J., Pellecchia, M., Schönbrunn, E., Cheng, J. Q., et al. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2010.63 · Cited by 93

Shepherding AKT and androgen receptor by Ack1 tyrosine kinase.

Mahajan, K., & Mahajan, N. P. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22162 · Cited by 92

Suppression of Hypoxia-Inducible Factor 2α Restores p53 Activity via Hdm2 and Reverses Chemoresistance of Renal Carcinoma Cells

Roberts, A. M., Watson, I. R., Evans, A. J., Foster, D. A., Irwin, M. S., & Ohh, M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1770 · Cited by 88

Activation of Extracellular Signal‐Regulated Kinase (ERK) and Akt by Human Serotonin 5‐HT 1B Receptors in Transfected BE(2)‐C Neuroblastoma Cells Is Inhibited by RGS4

Lione, A. M., Errico, M., Lin, S. L., & Cowen, D. S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750934.x · Cited by 73

SGK1 Kinase Upregulates GLUT1 Activity and Plasma Membrane Expression

Palmada, M., Boehmer, C., Akel, A., Rajamanickam, J., Jeyaraj, S., Keller, K., & Lang, F. (2006) · Diabetes · doi:10.2337/diabetes.55.02.06.db05-0720 · Cited by 71

Akt acutely activates the cholesterogenic transcription factor SREBP-2

Luu, W., Sharpe, L. J., Stevenson, J., & Brown, A. J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.017 · Cited by 68

Heparanase, cell signaling, and viral infections

Koganti, R., Suryawanshi, R., & Shukla, D. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03559-y · Cited by 67