AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control

mTOR Signaling in Growth, Metabolism, and Disease

Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555

AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1

Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227

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

AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint

Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300

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 3,051

Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy

Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600

AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α

Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491

Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids

Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464

A mammalian protein targeted by G1-arresting rapamycin–receptor complex

Brown, E. J., Albers, M. W., Bum Shin, T., ichikawa, K., Keith, C. T., Lane, W. S., & Schreiber, S. L. (1994) · Nature · doi:10.1038/369756a0 · Cited by 2,053

Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast

Heitman, J., Movva, N. R., & Hall, M. N. (1991) · Science · doi:10.1126/science.1715094 · Cited by 2,010

A lysosome‐to‐nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB

Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Erdin, S., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,920

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

On the origin of mitosing cells

Sagan, L. (1967) · Journal of Theoretical Biology · doi:10.1016/0022-5193(67)90079-3 · Cited by 1,870

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

The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress

Shaw, R. J., Kosmatka, M., Bardeesy, N., Hurley, R. L., Witters, L. A., DePinho, R. A., & Cantley, L. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308061100 · Cited by 1,797

Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade

Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Mäkelä, T. P., Alessi, D. R., & Hardie, D. G. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-28 · Cited by 1,694

mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase

Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673

LKB1 is the upstream kinase in the AMP-activated protein kinase cascade

Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650

Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.009 · Cited by 1,589

A central integrator of transcription networks in plant stress and energy signalling

Gonzalez, E. B., Rolland, F., Thevelein, J. M., & Sheen, J. (2007) · Nature · doi:10.1038/nature06069 · Cited by 1,526

RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs

Sabatini, D. M., Erdjument-Bromage, H., Lui, M., Tempst, P., & Snyder, S. H. (1994) · Cell · doi:10.1016/0092-8674(94)90570-3 · Cited by 1,509

Ca2+/calmodulin-dependent protein kinase kinase-β acts upstream of AMP-activated protein kinase in mammalian cells

Woods, A., Dickerson, K., Heath, R. B., Hong, S. P., Momcilovic, M., Johnstone, S. R., Carlson, M., & Carling, D. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.005 · Cited by 1,418

The Transcription Factor TFEB Links mTORC1 Signaling to Transcriptional Control of Lysosome Homeostasis

Roczniak-Ferguson, A., Petit, C. S. V., Froehlich, F., Qian, S., Ky, J., Angarola, B. L., Walther, T. C., & Ferguson, S. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002790 · Cited by 1,393

LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1

Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J., Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600110 · Cited by 1,381

MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB

Martina, J. A., Chen, Y., Gucek, M., & Puertollano, R. (2012) · Autophagy · doi:10.4161/auto.19653 · Cited by 1,333

Sestrin2 is a leucine sensor for the mTORC1 pathway

Wolfson, R. L., Chantranupong, L., Saxton, R. A., Shen, K., Scaria, S. M., Cantor, J. R., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aab2674 · Cited by 1,306

The energetics of genome complexity.

Lane, N., & Martin, W. (2010) · Nature · doi:10.1038/nature09486 · Cited by 1,289

Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase

Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264

mTOR as a central hub of nutrient signalling and cell growth

Kim, J., & Guan, K. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0205-1 · Cited by 1,094

AMP-activated protein kinase mediates mitochondrial fission in response to energy stress

Toyama, E. Q., Herzig, S., Courchet, J., Lewis, T. L., Losón, O. C., Hellberg, K., Young, N. P., Chen, H., Polleux, F., Chan, D. C., et al. (2016) · Science · doi:10.1126/science.aab4138 · Cited by 1,085

A Tumor Suppressor Complex with GAP Activity for the Rag GTPases That Signal Amino Acid Sufficiency to mTORC1

Bar-Peled, L., Chantranupong, L., Cherniack, A. D., Chen, W. W., Ottina, K. A., Grabiner, B. C., Spear, E. D., Carter, S. L., Meyerson, M., & Sabatini, D. M. (2013) · Science · doi:10.1126/science.1232044 · Cited by 1,080

mTOR kinase structure, mechanism and regulation

Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., & Pavletich, N. P. (2013) · Nature · doi:10.1038/nature12122 · Cited by 1,075

LKB1 modulates lung cancer differentiation and metastasis

Ji, H., Ramsey, M. R., Hayes, D. N., Fan, C., McNamara, K., Kozlowski, P., Torrice, C., Wu, M. C., Shimamura, T., Perera, S. A., et al. (2007) · Nature · doi:10.1038/nature06030 · Cited by 1,064

Making new contacts: the mTOR network in metabolism and signalling crosstalk

Shimobayashi, M., & Hall, M. N. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3757 · Cited by 1,053

AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation

Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., & Shulman, G. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625599 · Cited by 1,036

Rapamycin passes the torch: a new generation of mTOR inhibitors

Benjamin, D., Colombi, M., Moroni, C., & Hall, M. N. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3531 · Cited by 1,013

Rheb Binds and Regulates the mTOR Kinase

Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., & Avruch, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.053 · Cited by 1,005

The Ca2+/Calmodulin-dependent Protein Kinase Kinases Are AMP-activated Protein Kinase Kinases

Hurley, R. L., Anderson, K. A., Franzone, J. M., Kemp, B. E., Means, A. R., & Witters, L. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503824200 · Cited by 1,004

Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome

Cool, B. L., Zinker, B. A., Chiou, W. J. H., Kifle, L., Cao, N., Perham, M., Dickinson, R., Adler, A. L., Gagné, G. D., Iyengar, R., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.005 · Cited by 939

A hierarchy of ATP-consuming processes in mammalian cells

Buttgereit, F., & Brand, M. D. (1995) · Biochemical Journal · doi:10.1042/bj3120163 · Cited by 939

Structure of mammalian AMPK and its regulation by ADP

Xiao, B., Sanders, M. J., Underwood, E., Heath, R., Mayer, F. V., Carmena, D., Jing, C., Walker, P. A., Eccleston, J. F., Haire, L. F., et al. (2011) · Nature · doi:10.1038/nature09932 · Cited by 926

Ragulator Is a GEF for the Rag GTPases that Signal Amino Acid Levels to mTORC1

Bar-Peled, L., Schweitzer, L. D., Zoncu, R., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.07.032 · Cited by 918

The Mouse Locus Encodes Axin, an Inhibitor of the Wnt Signaling Pathway That Regulates Embryonic Axis Formation

Zeng, L., Fagotto, F., Zhang, T., Hsu, W., Vasicek, T. J., Perry, W. L., Lee, J. J., Tilghman, S. M., Gumbiner, B. M., & Costantini, F. D. (1997) · Cell · doi:10.1016/s0092-8674(00)80324-4 · Cited by 907

Single phosphorylation sites in Acc1 and Acc2 regulate lipid homeostasis and the insulin-sensitizing effects of metformin

Fullerton, M. D., Galic, S., Marcinko, K., Sikkema, S., Pulinilkunnil, T., Chen, Z.-P., O'Neill, H. M., Ford, R. J., Palanivel, R., O'Brien, M., et al. (2013) · Nature Medicine · doi:10.1038/nm.3372 · Cited by 893

Metformin, independent of AMPK, inhibits mTORC1 in a rag GTPase-dependent manner

Kalender, A., Selvaraj, A., Kim, S. Y., Gulati, P., Brûlé, S., Viollet, B., Kemp, B. E., Bardeesy, N., Dennis, P., Schlager, J. J., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.03.014 · Cited by 889

Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells

Sabers, C. J., Martin, M. M., Brunn, G. J., Williams, J. M., Dumont, F. J., Wiederrecht, G., & Abraham, R. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.815 · Cited by 887

Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1

Wang, S., Tsun, Z.-Y., Wolfson, R. L., Shen, K., Wyant, G. A., Plovanich, M., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 865

AMPK: An Energy-Sensing Pathway with Multiple Inputs and Outputs

Hardie, D. G., Schaffer, B. E., & Brunet, A. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.013 · Cited by 859

Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia

Marsin, A.-S., Bertrand, L., Rider, M. H., Deprez, J., Beauloye, C., Vincent, M. F., den Berghe, G. V., Carling, D., & Hue, L. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00742-9 · Cited by 853

The Energy Sensor AMP-activated Protein Kinase Directly Regulates the Mammalian FOXO3 Transcription Factor

Greer, E. L., Oskoui, P. R., Banko, M. R., Maniar, J. M., Gygi, M. P., Gygi, S. P., & Brunet, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705325200 · Cited by 852

The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway

Chantranupong, L., Scaria, S. M., Saxton, R. A., Gygi, M. P., Shen, K., Wyant, G. A., Wang, T., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.035 · Cited by 843

Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression

Kunz, J., Henríquez, R., Schneider, U., Deuter‐Reinhard, M., Movva, N. R., & Hall, M. N. (1993) · Cell · doi:10.1016/0092-8674(93)90144-f · Cited by 838

Differential Regulation of Distinct Vps34 Complexes by AMPK in Nutrient Stress and Autophagy

Kim, J., Kim, Y. C., Fang, C., Russell, R. C., Kim, J. H., Fan, W., Liu, R., Zhong, Q., & Guan, K. (2013) · Cell · doi:10.1016/j.cell.2012.12.016 · Cited by 829

LKB1-Dependent Signaling Pathways

Alessi, D. R., Sakamoto, K., & Bayascas, J. R. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142702 · Cited by 805

Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise

Winder, W. W., & Hardie, D. G. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.270.2.e299 · Cited by 799

mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle

Ben-Sahra, I., Hoxhaj, G., Ricoult, S. J. H., Asara, J. M., & Manning, B. D. (2016) · Science · doi:10.1126/science.aad0489 · Cited by 795

Glutaminolysis Activates Rag-mTORC1 Signaling

Durán, R. V., Oppliger, W., Robitaille, A. M., Heiserich, L., Skendaj, R., Gottlieb, E., & Hall, M. N. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.043 · Cited by 766

Spatial Control of the TSC Complex Integrates Insulin and Nutrient Regulation of mTORC1 at the Lysosome

Menon, S., Dibble, C. C., Talbott, G., Hoxhaj, G., Valvezan, A. J., Takahashi, H., Cantley, L. C., & Manning, B. D. (2014) · Cell · doi:10.1016/j.cell.2013.11.049 · Cited by 766

The Ancient Drug Salicylate Directly Activates AMP-Activated Protein Kinase

Hawley, S. A., Fullerton, M. D., Ross, F. A., Schertzer, J. D., Chevtzoff, C., Walker, K. J., Peggie, M. W., Zibrova, D., Green, K. A., Mustard, K. J., et al. (2012) · Science · doi:10.1126/science.1215327 · Cited by 760

Differential regulation of mTORC1 by leucine and glutamine

Jewell, J. L., Kim, Y. C., Russell, R. C., Yu, F.-X., Park, H. W., Plouffe, S. W., Tagliabracci, V. S., & Guan, K.-L. (2015) · Science · doi:10.1126/science.1259472 · Cited by 757

CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations

Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754

Nutrient sensing and TOR signaling in yeast and mammals

González, A., & Hall, M. N. (2017) · The EMBO Journal · doi:10.15252/embj.201696010 · Cited by 752

Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1

Ben-Sahra, I., Howell, J. J., Asara, J. M., & Manning, B. D. (2013) · Science · doi:10.1126/science.1228792 · Cited by 739

Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK

Zhang, C., Hawley, S. A., Zong, Y., Li, M., Wang, Z., Gray, A., Ma, T., Cui, J., Feng, J.-W., Zhu, M., et al. (2017) · Nature · doi:10.1038/nature23275 · Cited by 730

5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle.

Kurth-Kraczek, E. J., Hirshman, M. F., Goodyear, L. J., & Winder, W. W. (1999) · Diabetes · doi:10.2337/diabetes.48.8.1667 · Cited by 715

Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle

Winder, W. W., Holmes, B. F., Rubink, D. S., Jensen, E. B., Chen, M., & Holloszy, J. O. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.6.2219 · Cited by 709

A Yeast Gene That Is Essential for Release from Glucose Repression Encodes a Protein Kinase

Celenza, J. L., & Carlson, M. (1986) · Science · doi:10.1126/science.3526554 · Cited by 688

AMPK-Dependent Degradation of TXNIP upon Energy Stress Leads to Enhanced Glucose Uptake via GLUT1

Wu, N., Zheng, B., Shaywitz, A. J., Dagon, Y., Tower, C., Bellinger, G., Shen, C., Wen, J., Asara, J. M., McGraw, T. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.035 · Cited by 687

The Mammalian Target of Rapamycin (mTOR) Partner, Raptor, Binds the mTOR Substrates p70 S6 Kinase and 4E-BP1 through Their TOR Signaling (TOS) Motif

Nojima, H., Tokunaga, C., Eguchi, S., Oshiro, N., Sujuti, H., Yoshino, K., Hara, K., Tanaka, N., Avruch, J., & Yonezawa, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200665200 · Cited by 678

Self-renewing diploid Axin2+ cells fuel homeostatic renewal of the liver

Wang, B., Zhao, L., Fish, M., Logan, C. Y., & Nusse, R. (2015) · Nature · doi:10.1038/nature14863 · Cited by 674

SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673

mTORC1 signaling and the metabolic control of cell growth

Ben‐Sahra, I., & Manning, B. D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.012 · Cited by 668

The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans

Apfeld, J., O'Connor, G., McDonagh, T., DiStefano, P. S., & Curtis, R. (2004) · Genes & Development · doi:10.1101/gad.1255404 · Cited by 643

The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR

Egan, D., Kim, J., Shaw, R. J., & Guan, K.-L. (2011) · Autophagy · doi:10.4161/auto.7.6.15123 · Cited by 627

Inactivation of LKB1/STK11 is a common event in adenocarcinomas of the lung.

Sánchez‐Céspedes, M., Parrella, P., Esteller, M., Nomoto, S., Trink, B., Engles, J. M., Westra, W. H., Herman, J. G., & Sidransky, D. (2002) · PubMed · Cited by 626

Convergent energy and stress signaling

Gonzalez, E. B., & Sheen, J. (2008) · Trends in Plant Science · doi:10.1016/j.tplants.2008.06.006 · Cited by 622

TBC1D7 Is a Third Subunit of the TSC1-TSC2 Complex Upstream of mTORC1

Dibble, C. C., Elis, W., Menon, S., Qin, W., Klekota, J., Asara, J. M., Finan, P. M., Kwiatkowski, D. J., Murphy, L. O., & Manning, B. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.009 · Cited by 612

AMPK is a direct adenylate charge-regulated protein kinase

Oakhill, J. S., Steel, R., Chen, Z.-P., Scott, J. W., Ling, N., Tam, S., & Kemp, B. E. (2011) · Science · doi:10.1126/science.1200094 · Cited by 612

A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis

Carling, D., Zammit, V. A., & Hardie, D. G. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80292-2 · Cited by 599

SAMTOR is an S -adenosylmethionine sensor for the mTORC1 pathway

Gu, X., Orozco, J. M., Saxton, R. A., Condon, K. J., Liu, G. Y., Krawczyk, P. A., Scaria, S. M., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2017) · Science · doi:10.1126/science.aao3265 · Cited by 598

5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2C α and native bovine protein phosphatase‐2A c

(1995) · FEBS Letters · doi:10.1016/0014-5793(95)01368-7 · Cited by 595 · cited 1×

Structural basis of AMPK regulation by small molecule activators

Xiao, B., Sanders, M. J., Carmena, D., Bright, N. J., Haire, L. F., Underwood, E., Patel, B. R., Heath, R. B., Walker, P. A., Hallén, S., et al. (2013) · Nature Communications · doi:10.1038/ncomms4017 · Cited by 566

The Folliculin Tumor Suppressor Is a GAP for the RagC/D GTPases That Signal Amino Acid Levels to mTORC1

Tsun, Z.-Y., Bar-Peled, L., Chantranupong, L., Zoncu, R., Wang, T., Kim, C., Spooner, E., & Sabatini, D. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.016 · Cited by 565

The Lysosomal v-ATPase-Ragulator Complex Is a Common Activator for AMPK and mTORC1, Acting as a Switch between Catabolism and Anabolism

Zhang, C., Jiang, B., Li, M., Zhu, M., Peng, Y., Zhang, Y., Wu, Y., Li, T. Y., Yu, L., Lu, Z., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.014 · Cited by 565

The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway

Wolfson, R. L., & Sabatini, D. M. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.07.001 · Cited by 563

SNF1/AMPK pathways in yeast

Hedbacker, K. (2008) · Frontiers in Bioscience · doi:10.2741/2854 · Cited by 554

Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40

Yang, H., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., & Pavletich, N. P. (2017) · Nature · doi:10.1038/nature25023 · Cited by 548

The structure of a domain common to archaebacteria and the homocystinuria disease protein.

Bateman, A. (1997) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(96)30046-7 · Cited by 544

AMP Is a True Physiological Regulator of AMP-Activated Protein Kinase by Both Allosteric Activation and Enhancing Net Phosphorylation

Gowans, G. J., Hawley, S. A., Ross, F. A., & Hardie, D. G. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.08.019 · Cited by 531

The complex relationship between TFEB transcription factor phosphorylation and subcellular localization

Puertollano, R., Ferguson, S. M., Brugarolas, J., & Ballabio, A. (2018) · The EMBO Journal · doi:10.15252/embj.201798804 · Cited by 530

TOS Motif-Mediated Raptor Binding Regulates 4E-BP1 Multisite Phosphorylation and Function

Schalm, S. S., Fingar, D. C., Sabatini, D. M., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00329-4 · Cited by 528

Quantitative Phosphoproteomics Reveal mTORC1 Activates de Novo Pyrimidine Synthesis

Robitaille, A. M., Christen, S., Shimobayashi, M., Cornu, M., Fava, L. L., Moes, S., Prescianotto-Baschong, C., Sauer, U., Jenoe, P., & Hall, M. N. (2013) · Science · doi:10.1126/science.1228771 · Cited by 525

PIK-Related Kinases: DNA Repair, Recombination, and Cell Cycle Checkpoints

Keith, C. T., & Schreiber, S. L. (1995) · Science · doi:10.1126/science.270.5233.50 · Cited by 521

Mammalian TAK1 Activates Snf1 Protein Kinase in Yeast and Phosphorylates AMP-activated Protein Kinase in Vitro

Momcilovic, M., Hong, S. P., & Carlson, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604399200 · Cited by 504

mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a Nutrient

Wyant, G. A., Abu-Remaileh, M., Wolfson, R. L., Chen, W. W., Freinkman, E., Danai, L. V., Heiden, M. G. V., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.09.046 · Cited by 494

Identification of a Conserved Motif Required for mTOR Signaling

Schalm, S. S., & Blenis, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00762-5 · Cited by 490

RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.

Chiu, M. I., Katz, H., & Berlin, V (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12574 · Cited by 481

Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival

Efeyan, A., Zoncu, R., Chang, S. H., Gumper, I., Snitkin, H., Wolfson, R. L., Kirak, O., Sabatini, D. M., & Sabatini, D. M. (2012) · Nature · doi:10.1038/nature11745 · Cited by 473

The Sestrins Interact with GATOR2 to Negatively Regulate the Amino-Acid-Sensing Pathway Upstream of mTORC1

Chantranupong, L., Wolfson, R. L., Orozco, J. M., Saxton, R. A., Scaria, S. M., Bar-Peled, L., Spooner, E., Isasa, M., Gygi, S. P., & Sabatini, D. M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.014 · Cited by 466

Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway

Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aad2087 · Cited by 457

Mechanism of Action of A-769662, a Valuable Tool for Activation of AMP-activated Protein Kinase

Göransson, O., McBride, A., Hawley, S. A., Ross, F. A., Shpiro, N., Foretz, M., Viollet, B., Hardie, D. G., & Sakamoto, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706536200 · Cited by 452

5′-AMP Activates the AMP-activated Protein Kinase Cascade, and Ca2+/Calmodulin Activates the Calmodulin-dependent Protein Kinase I Cascade, via Three Independent Mechanisms

Hawley, S. A., Selbert, M. A., Goldstein, E. G., Edelman, A. M., Carling, D., & Hardie, D. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27186 · Cited by 441

The Glycogen-Binding Domain on the AMPK β Subunit Allows the Kinase to Act as a Glycogen Sensor

McBride, A., Ghilagaber, S., Nikolaev, A., & Hardie, D. G. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.11.008 · Cited by 432

The Vam6 GEF Controls TORC1 by Activating the EGO Complex

Binda, M., Gulli, M., Bonfils, G., Panchaud, N., Urban, J., Sturgill, T. W., Loewith, R., & VIRGILIO, C. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.033 · Cited by 432

Hunger States Switch a Flip-Flop Memory Circuit via a Synaptic AMPK-Dependent Positive Feedback Loop

Yang, Y., Atasoy, D., Su, H. H., & Sternson, S. M. (2011) · Cell · doi:10.1016/j.cell.2011.07.039 · Cited by 431

AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen

Polekhina, G., Gupta, A., Michell, B. J., van Denderen, B., Murthy, S., Feil, S. C., Jennings, I. G., Campbell, D. J., Witters, L. A., Parker, M. W., et al. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00292-6 · Cited by 423

The lysosome turns fifty

Duve, C. D. (2005) · Nature Cell Biology · doi:10.1038/ncb0905-847 · Cited by 422

AMPK–SKP2–CARM1 signalling cascade in transcriptional regulation of autophagy

Shin, H.-J. R., Kim, H., Oh, S., Lee, J.-G., Kee, M., Ko, H.-J., Kweon, M.-N., Won, K.-J., & Baek, S. H. (2016) · Nature · doi:10.1038/nature18014 · Cited by 417

Regulation of TORC1 in Response to Amino Acid Starvation via Lysosomal Recruitment of TSC2

Demetriades, C., Doumpas, N., & Teleman, A. A. (2014) · Cell · doi:10.1016/j.cell.2014.01.024 · Cited by 414

Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo.

Woods, A., Munday, M. R., Scott, J., Yang, X., Carlson, M., & Carling, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32198-1 · Cited by 409

AMP-activated protein kinase (AMPK) β1β2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise

O'Neill, H. M., Maarbjerg, S. J., Crane, J. D., Jeppesen, J., Jørgensen, S. B., Schertzer, J. D., Shyroka, O., Kiens, B., van Denderen, B. J., Tarnopolsky, M. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105062108 · Cited by 406

TAK1 activates AMPK‐dependent cytoprotective autophagy in TRAIL‐treated epithelial cells

Herrero‐Martín, G., Høyer‐Hansen, M., García‐García, C., Fumarola, C., Farkas, T., López‐Rivas, A., & Jäättelä, M. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.8 · Cited by 400

Nutrient acquisition strategies of mammalian cells

Palm, W., & Thompson, C. B. (2017) · Nature · doi:10.1038/nature22379 · Cited by 388

AMP ‐activated protein kinase: a cellular energy sensor that comes in 12 flavours

Ross, F. A., MacKintosh, C., & Hardie, D. G. (2016) · The FEBS Journal · doi:10.1111/febs.13698 · Cited by 381

The Stimulation of Glycolysis by Hypoxia in Activated Monocytes Is Mediated by AMP-activated Protein Kinase and Inducible 6-Phosphofructo-2-kinase

Marsin, A.-S., Bouzin, C., Bertrand, L., & Hue, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205213200 · Cited by 380

Structure of the LKB1-STRAD-MO25 Complex Reveals an Allosteric Mechanism of Kinase Activation

Zeqiraj, E., Filippi, B., Deák, M., Alessi, D. R., & van Aalten, D. M. F. (2009) · Science · doi:10.1126/science.1178377 · Cited by 376

Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio

Wilson, W. A., Hawley, S. A., & Hardie, D. G. (1996) · Current Biology · doi:10.1016/s0960-9822(96)00747-6 · Cited by 375

Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases

Petit, C. S., Roczniak-Ferguson, A., & Ferguson, S. M. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201307084 · Cited by 355

Insulin Antagonizes Ischemia-induced Thr172 Phosphorylation of AMP-activated Protein Kinase α-Subunits in Heart via Hierarchical Phosphorylation of Ser485/491

Horman, S., Vertommen, D., Heath, R. B., Neumann, D., Mouton, V., Woods, A., Schlattner, U., Wallimann, T., Carling, D., Hue, L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506850200 · Cited by 355

Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family

Sanders, M. J., Ali, Z. S., Hegarty, B. D., Heath, R., Snowden, M. A., & Carling, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706543200 · Cited by 347

Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation

Nukarinen, E., Nägele, T., Pedrotti, L., Wurzinger, B., Mair, A., Landgraf, R., Börnke, F. A. J., Hanson, J., Teige, M., Gonzalez, E. B., et al. (2016) · Scientific Reports · doi:10.1038/srep31697 · Cited by 347

Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy

Myers, R. W., Guan, H.-P., Ehrhart, J., Petrov, A., Prahalada, S., Tozzo, E., Yang, X., Kurtz, M. M., Trujillo, M., Gonzalez Trotter, D., et al. (2017) · Science · doi:10.1126/science.aah5582 · Cited by 346

Cell Cycle Regulation via p53 Phosphorylation by a 5′-AMP Activated Protein Kinase Activator, 5-Aminoimidazole- 4-Carboxamide-1-β- -Ribofuranoside, in a Human Hepatocellular Carcinoma Cell Line

Imamura, K., Ogura, T., Kishimoto, A., Kaminishi, M., & Esumi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5627 · Cited by 345

KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1

Wolfson, R. L., Chantranupong, L., Wyant, G. A., Gu, X., Orozco, J. M., Shen, K., Condon, K. J., Petri, S., Kedir, J. F., Scaria, S. M., et al. (2017) · Nature · doi:10.1038/nature21423 · Cited by 345

Architecture of human mTOR complex 1

Aylett, C. H. S., Sauer, E., Imseng, S., Boehringer, D., Hall, M. N., Ban, N., & Maier, T. (2016) · Science · doi:10.1126/science.aaa3870 · Cited by 344

Snf1 Protein Kinase Regulates Phosphorylation of the Mig1 Repressor in Saccharomyces cerevisiae

Treitel, M. A., Kuchin, S., & Carlson, M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6273 · Cited by 343

The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK–ERK pathway to late endosomes

Nada, S., Hondo, A., Kasai, A., Koike, M., Saito, K., Uchiyama, Y., & Okada, M. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.308 · Cited by 341

Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase.

Mitchelhill, K. I., Stapleton, D., Gao, G., House, C. M., Michell, B. J., Katsis, F., Witters, L. A., & Kemp, B. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41951-x · Cited by 338

Sestrins inhibit mTORC1 kinase activation through the GATOR complex

Parmigiani, A., Nourbakhsh, A., Ding, B., Wang, W., Kim, Y. C., Akopiants, K., Guan, K.-L., Karin, M., & Budanov, A. V. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.019 · Cited by 336

A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias

Hudson, E. R., Pan, D. A., James, J., Lucocq, J. M., Hawley, S. A., Green, K. A., Baba, O., Terashima, T., & Hardie, D. G. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00249-5 · Cited by 332

Mechanism of arginine sensing by CASTOR1 upstream of mTORC1

Saxton, R. A., Chantranupong, L., Knockenhauer, K. E., Schwartz, T. U., & Sabatini, D. M. (2016) · Nature · doi:10.1038/nature19079 · Cited by 308

p70S6 Kinase Phosphorylates AMPK on Serine 491 to Mediate Leptin's Effect on Food Intake

Dagon, Y., Hur, E. E., Zheng, B., Wellenstein, K., Cantley, L. C., & Kahn, B. B. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.05.010 · Cited by 297

Activation of GLUT1 by metabolic and osmotic stress: potential involvement of AMP-activated protein kinase (AMPK)

Barnes, K., Ingram, J. C., Porras, O. H., Barros, L. F., Hudson, E. R., Fryer, L. G. D., Foufelle, F., Carling, D., Hardie, D. G., & Baldwin, S. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.11.2433 · Cited by 289

Two SNF1-Related Protein Kinases from Spinach Leaf Phosphorylate and Inactivate 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase, Nitrate Reductase, and Sucrose Phosphate Synthase in Vitro1

Sugden, C., Donaghy, P. G., Halford, N. G., & Hardie, D. G. (1999) · PLANT PHYSIOLOGY · doi:10.1104/pp.120.1.257 · Cited by 288

Amino Acid Deprivation Inhibits TORC1 Through a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr1

Panchaud, N., Péli-Gulli, M.-P., & De Virgilio, C. (2013) · Science Signaling · doi:10.1126/scisignal.2004112 · Cited by 286

AMP as a Low-Energy Charge Signal Autonomously Initiates Assembly of AXIN-AMPK-LKB1 Complex for AMPK Activation

Zhang, Y., Guo, H., Zhang, C., Lin, S., Yin, Z., Peng, Y., Luo, H., Shi, Y., Lian, G., Zhang, C., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.09.005 · Cited by 278

Subcellular localization of the Snf1 kinase is regulated by specific β subunits and a novel glucose signaling mechanismPreprint

Vincent, O., Townley, R. A., Kuchin, S., et al. (2001) · Genes & Development · doi:10.1101/gad.879301 · Cited by 277

Activation of Skeletal Muscle AMPK Promotes Glucose Disposal and Glucose Lowering in Non-human Primates and Mice

Cokorinos, E., Delmore, J. E., Reyes, A. R., Albuquerque, B., Kjøbsted, R., Eskesen, N. O., Tran, J.-L., Jatkar, A., Cialdea, K., Esquejo, R. M., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.010 · Cited by 272

Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9

Jung, J., Genau, H. M., & Behrends, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00125-15 · Cited by 266

Regulation of AMP-activated Protein Kinase by Multisite Phosphorylation in Response to Agents That Elevate Cellular cAMP

Hurley, R. L., Barré, L. K., Wood, S. D., Anderson, K. A., Kemp, B. E., Means, A. R., & Witters, L. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606676200 · Cited by 264

Leucine Signals to mTORC1 via Its Metabolite Acetyl-Coenzyme A

Son, S. M., Park, S. J., Lee, H., Siddiqi, F. H., Lee, J. E., Menzies, F. M., & Rubinsztein, D. C. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.08.013 · Cited by 250

The α2–5′AMP-Activated Protein Kinase Is a Site 2 Glycogen Synthase Kinase in Skeletal Muscle and Is Responsive to Glucose Loading

Jørgensen, S. B., Nielsen, J. N., Birk, J. B., Olsen, G. S., Viollet, B., Andreelli, F., Schjerling, P., Vaulont, S., Hardie, D. G., Hansen, B. F., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.12.3074 · Cited by 241

Mutations in the Arabidopsis Homolog of LST8/GβL, a Partner of the Target of Rapamycin Kinase, Impair Plant Growth, Flowering, and Metabolic Adaptation to Long Days

Moreau, M., Azzopardi, M., Clément, G., Dobrenel, T., Marchive, C., Renne, C., Martin‐Magniette, M., Soubigou‐Taconnat, L., Renou, J., Robaglia, C., et al. (2012) · The Plant Cell · doi:10.1105/tpc.111.091306 · Cited by 238

Inhibition of AMPK Catabolic Action by GSK3

Suzuki, T., Bridges, D., Nakada, D., Skiniotis, G., Morrison, S. J., Lin, J. D., Saltiel, A. R., & Inoki, K. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.022 · Cited by 232

Phosphorylation by Akt within the ST loop of AMPK-α1 down-regulates its activation in tumour cells

Hawley, S. A., Ross, F. A., Gowans, G. J., Tibarewal, P., Leslie, N. R., & Hardie, D. G. (2014) · Biochemical Journal · doi:10.1042/bj20131344 · Cited by 229

AMPK controls exercise endurance, mitochondrial oxidative capacity, and skeletal muscle integrity.

Lantier, L., Fentz, J., Mounier, R., Leclerc, J., Treebak, J. T., Pehmøller, C., Sanz, N., Sakakibara, I., Saint‐Amand, E., Rimbaud, S., et al. (2014) · The FASEB Journal · doi:10.1096/fj.14-250449 · Cited by 228

AMPK directly activates mTORC2 to promote cell survival during acute energetic stress

Kazyken, D., Magnuson, B., Bodur, Ç., Acosta-Jaquez, H. A., Zhang, D., Tong, X., Barnes, T. M., Steinl, G. K., Patterson, N., Altheim, C. H., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aav3249 · Cited by 226

AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply

Hoppe, S., Bierhoff, H., Cado, I., Weber, A., Tiebe, M., Grummt, I., & Voit, R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909873106 · Cited by 225

The eukaryotic linear motif resource – 2018 update

Gouw, M., Michael, S., Sámano‐Sánchez, H., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1077 · Cited by 219

Ionizing Radiation Activates AMP-Activated Kinase (AMPK): A Target for Radiosensitization of Human Cancer Cells

Sanli, T., Rashid, A., Liu, C., Harding, S. M., Bristow, R. G., Cutz, J.-C., Singh, G., Wright, J. R., & Tsakiridis, T. K. (2010) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2010.03.005 · Cited by 216

Thrombin Activates AMP-Activated Protein Kinase in Endothelial Cells via a Pathway Involving Ca2+/Calmodulin-Dependent Protein Kinase Kinase β

Stahmann, N., Woods, A., Carling, D., & Heller, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00383-06 · Cited by 214

Structural basis for the docking of mTORC1 on the lysosomal surface

Rogala, K. B., Gu, X., Kedir, J. F., Abu-Remaileh, M., Bianchi, L. F., Bottino, A. M. S., Dueholm, R., Niehaus, A., Overwijn, D., Fils, A.-C. P., et al. (2019) · Science · doi:10.1126/science.aay0166 · Cited by 214

Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA.

Alderson, A. L., Sabelli, P. A., Dickinson, J. R., Cole, D., Richardson, M., Kreis, M. E., Shewry, P. R., & Halford, N. G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8602 · Cited by 209

The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae

DeVit, M. J., & Johnston, M. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80503-x · Cited by 201

Structural insight into the autoinhibition mechanism of AMP-activated protein kinase

Chen, L., Jiao, Z., Zheng, L., Zhang, Y., Xie, S.-T., Wang, Z., & Wu, J. (2009) · Nature · doi:10.1038/nature08075 · Cited by 200

Structural basis of AMPK regulation by adenine nucleotides and glycogen

Li, X., Wang, L., Zhou, X. E., Ke, J., de Waal, P. W., Gu, X., Tan, M. H. E., Wang, D., Wu, D., Xu, H. E., et al. (2014) · Cell Research · doi:10.1038/cr.2014.150 · Cited by 198

Regulation of mTOR Complex 1 (mTORC1) by Raptor Ser863 and Multisite Phosphorylation

Foster, K. G., Acosta-Jaquez, H. A., Roméo, Y., Üstünel, B. E., Soliman, G. A., Carriere, A., Roux, P. P., Ballif, B. A., & Fingar, D. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.029637 · Cited by 197

Activation of mTORC1 is essential for β-adrenergic stimulation of adipose browning

Liu, D., Bordicchia, M., Zhang, C., Fang, H., Wei, W., Li, J., Guilherme, A., Guntur, K., Czech, M., & Collins, S. (2016) · Journal of Clinical Investigation · doi:10.1172/jci83532 · Cited by 197

Regulation of spinach SNF1‐related (SnRK1) kinases by protein kinases and phosphatases is associated with phosphorylation of the T loop and is regulated by 5′‐AMP

Sugden, C., Crawford, R. M., Halford, N. G., & Hardie, D. G. (1999) · The Plant Journal · doi:10.1046/j.1365-313x.1999.00532.x · Cited by 195

SZT2 dictates GATOR control of mTORC1 signalling

Peng, M., Yin, N., & Li, M. O. (2017) · Nature · doi:10.1038/nature21378 · Cited by 192

Architecture of the human GATOR1 and GATOR1–Rag GTPases complexes

Shen, K., Huang, R. K., Brignole, E. J., Condon, K. J., Valenstein, M. L., Chantranupong, L., Bomaliyamu, A., Choe, A., Hong, C., Yu, Z., et al. (2018) · Nature · doi:10.1038/nature26158 · Cited by 192

Structural Basis for Glycogen Recognition by AMP-Activated Protein Kinase

Polekhina, G., Gupta, A., van Denderen, B. J. W., Feil, S. C., Kemp, B. E., Stapleton, D., & Parker, M. W. (2005) · Structure · doi:10.1016/j.str.2005.07.008 · Cited by 191

Structural Basis for AMPK Activation: Natural and Synthetic Ligands Regulate Kinase Activity from Opposite Poles by Different Molecular Mechanisms

Calabrese, M. F., Rajamohan, F., Harris, M. S., Caspers, N. L., Magyar, R. A., Withka, J. M., Wang, H., Borzilleri, K. A., Sahasrabudhe, P. V., Hoth, L. R., et al. (2014) · Structure · doi:10.1016/j.str.2014.06.009 · Cited by 185

Identification of AMPK Phosphorylation Sites Reveals a Network of Proteins Involved in Cell Invasion and Facilitates Large-Scale Substrate Prediction

Schaffer, B. E., Levin, R. S., Hertz, N. T., Maures, T. J., Schoof, M. L., Hollstein, P. E., Benayoun, B. A., Banko, M. R., Shaw, R. J., Shokat, K. M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.009 · Cited by 184

Etoposide Induces ATM-Dependent Mitochondrial Biogenesis through AMPK Activation

Fu, X., Wan, S., Lyu, Y. L., Liu, L. F., & Qi, H. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002009 · Cited by 183

Sestrin2 inhibits mTORC1 through modulation of GATOR complexes

Kim, J. S., Ro, S., Kim, M.-J., Park, H., Semple, I. A., Park, H., Cho, U., Wang, W., Guan, K., Karin, M., et al. (2015) · Scientific Reports · doi:10.1038/srep09502 · Cited by 180

The AMP-activated protein kinase: a multisubstrate regulator of lipid metabolism

Hardie, D. G., Carling, D., & Sim, A. T. R. (1989) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(89)90084-4 · Cited by 175

Differential regulation by AMP and ADP of AMPK complexes containing different γ subunit isoforms

Ross, F. A., Jensen, T. E., & Hardie, D. G. (2016) · Biochemical Journal · doi:10.1042/bj20150910 · Cited by 172

Genetic disruption of AMPK signaling abolishes both contraction- and insulin-stimulated TBC1D1 phosphorylation and 14-3-3 binding in mouse skeletal muscle

Pehmøller, C., Treebak, J. T., Birk, J. B., Chen, S., MacKintosh, C., Hardie, D. G., Richter, E. A., & Wojtaszewski, J. F. P. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00115.2009 · Cited by 171

ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase

Mayer, F. V., Heath, R. B., Underwood, E., Sanders, M. J., Carmena, D., McCartney, R. R., Leiper, F. C., Xiao, B., Jing, C., Walker, P. A., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.09.009 · Cited by 169

Small Molecule Drug A-769662 and AMP Synergistically Activate Naive AMPK Independent of Upstream Kinase Signaling

Scott, J. W., Ling, N. X. Y., Issa, S. M. A., Dite, T. A., O’Brien, M. T., Chen, Z., Galić, S., Langendorf, C. G., Steinberg, G. R., Kemp, B. E., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.03.006 · Cited by 169

Identification of the sucrose non‐fermenting related kinase SNRK, as a novel LKB1 substrate

Jaleel, M., McBride, A., Lizcano, J. M., Deák, M., Toth, R. L., MORRICE, N. A., & Alessi, D. R. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.042 · Cited by 168

Hierarchical activation of compartmentalized pools of AMPK depends on severity of nutrient or energy stress

Zong, Y., Zhang, C., Li, M., Wang, W., Wang, Z., Hawley, S. A., Ma, T., Feng, J.-W., Tian, X., Qu, Q., et al. (2019) · Cell Research · doi:10.1038/s41422-019-0163-6 · Cited by 168

Motif affinity and mass spectrometry proteomic approach for the discovery of cellular AMPK targets: Identification of mitochondrial fission factor as a new AMPK substrate

Ducommun, S., Deak, M., Sumpton, D., Ford, R. J., Núñez Galindo, A., Kussmann, M., Viollet, B., Steinberg, G. R., Foretz, M., Dayon, L., et al. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.008 · Cited by 167

Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms

Shen, K., & Sabatini, D. M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811727115 · Cited by 165

Lysosomal recruitment of TSC2 is a universal response to cellular stress

Demetriades, C., Plescher, M., & Teleman, A. A. (2016) · Nature Communications · doi:10.1038/ncomms10662 · Cited by 160

Snf1‐related protein kinase 1 is needed for growth in a normal day–night light cycle

Thelander, M., Olsson, T., & Ronne, H. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600182 · Cited by 155

Regulation of rat liver acetyl-CoA carboxylase. Regulation of phosphorylation and inactivation of acetyl-CoA carboxylase by the adenylate energy charge.

Yeh, L.-A., Lee, K. H., & Kim, K. H. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85891-x · Cited by 153

Evolution of the TOR Pathway

van Dam, T. J. P., Zwartkruis, F. J. T., Bos, J. L., & Snel, ‎. (2011) · Journal of Molecular Evolution · doi:10.1007/s00239-011-9469-9 · Cited by 147

Architecture of human Rag GTPase heterodimers and their complex with mTORC1

Anandapadamanaban, M., Masson, G. R., Perisic, O., Berndt, A., Kaufman, J., Johnson, C. M., Santhanam, B., Rogala, K. B., Sabatini, D. M., & Williams, R. L. (2019) · Science · doi:10.1126/science.aax3939 · Cited by 147

Transient Receptor Potential V Channels Are Essential for Glucose Sensing by Aldolase and AMPK

Li, M., Zhang, C., Zong, Y., Feng, J.-W., Ma, T., Hu, M., Lin, Z., Li, X., Xie, C., Wu, Y., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.05.018 · Cited by 144

Molecular Basis of the Rapamycin Insensitivity of Target Of Rapamycin Complex 2

Gaubitz, C., Oliveira, T. M., Prouteau, M., Leitner, A., Karuppasamy, M., Konstantinidou, G., Rispal, D., Eltschinger, S., Robinson, G. C., Thore, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.04.031 · Cited by 142

HIF-independent role of prolyl hydroxylases in the cellular response to amino acids

Durán, R. V., MacKenzie, E. D., Boulahbel, H., Frezza, C., Heiserich, L., Tardito, S., Bussolati, O., Rocha, S., Hall, M. N., & Gottlieb, E. (2013) · Oncogene · doi:10.1038/onc.2012.465 · Cited by 139

Phosphatidic Acid Activates Mammalian Target of Rapamycin Complex 1 (mTORC1) Kinase by Displacing FK506 Binding Protein 38 (FKBP38) and Exerting an Allosteric Effect

Yoon, M., Sun, Y., Arauz, E. J., Jiang, Y., & Chen, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.262816 · Cited by 138

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

The Snf1 kinase controls glucose repression in yeast by modulating interactions between the Mig1 repressor and the Cyc8‐Tup1 co‐repressor

Papamichos‐Chronakis, M., Gligoris, T. G., & Tzamarias, D. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400120 · Cited by 133

AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase

Bultot, L., Guigas, B., Von Wilamowitz-Moellendorff, A., Maisin, L., Vertommen, D., Hussain, N., Beullens, M., Guinovart, J. J., Foretz, M., Viollet, B., et al. (2012) · Biochemical Journal · doi:10.1042/bj20112026 · Cited by 131

Evolutionary Conservation of the Components in the TOR Signaling Pathways

Tatebe, H., & Shiozaki, K. (2017) · Biomolecules · doi:10.3390/biom7040077 · Cited by 130

The kinase triad, AMPK, mTORC1 and ULK1, maintains energy and nutrient homoeostasis

Dunlop, E. A., & Tee, A. R. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130030 · Cited by 123

TORC1 organized in inhibited domains (TOROIDs) regulate TORC1 activity

Prouteau, M., Desfosses, A., Sieben, C., Bourgoint, C., Mozaffari, N. L., Demurtas, D., MITRA, A. K., Guichard, P., Manley, S., & Loewith, R. (2017) · Nature · doi:10.1038/nature24021 · Cited by 122

Mammalian Target of Rapamycin Complex 1 (mTORC1) Activity Is Associated with Phosphorylation of Raptor by mTOR

Wang, L., Lawrence, J. C., Sturgill, T. W., & Harris, T. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.002907 · Cited by 121

Mouse Axin and Axin2/Conductin Proteins Are Functionally Equivalent In Vivo

Chia, I. V., & Costantini, F. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.11.4371-4376.2005 · Cited by 121

Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl Coenzyme A reductase kinase by adenosine 5′-monophosphate

Ferrer, A., Caelles, C., Massot, N., & Hegardt, F. G. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)91161-1 · Cited by 118

Complete avian malaria parasite genomes reveal features associated with lineage-specific evolution in birds and mammalsPreprint

Böhme, U., Otto, T. D., Cotton, J. A., Steinbiss, S., Sanders, M. J., Oyola, S. O., Nicot, A., Gandon, S., Patra, K. P., Herd, C., et al. (2018) · Genome Research · doi:10.1101/gr.218123.116 · Cited by 117

SEACing the GAP that nEGOCiates TORC1 activation

Panchaud, N., Gulli, M., & VIRGILIO, C. D. (2013) · Cell Cycle · doi:10.4161/cc.26000 · Cited by 115

GPCR signaling inhibits mTORC1 via PKA phosphorylation of Raptor

Jewell, J. L., Fu, V. X., Hong, A. W., Yu, F., Meng, D., Melick, C. H., Wang, H., Lam, W.-L. M., Yuan, H.-X., Taylor, S. S., et al. (2019) · eLife · doi:10.7554/elife.43038 · Cited by 115

A homologue of AMP-activated protein kinase in Drosophila melanogaster is sensitive to AMP and is activated by ATP depletion

Pan, D. A., & Hardie, D. G. (2002) · Biochemical Journal · doi:10.1042/bj20020703 · Cited by 112

Snf1/AMPK promotes the formation of Kog1/Raptor-bodies to increase the activation threshold of TORC1 in budding yeast

Hallett, J. E. H., Luo, X., & Capaldi, A. P. (2015) · eLife · doi:10.7554/elife.09181 · Cited by 112

Autophagy in inflammation, infection, and immunometabolism

Deretic, V. (2021) · Immunity · doi:10.1016/j.immuni.2021.01.018 · Cited by 862

Signaling pathways involved in colorectal cancer: pathogenesis and targeted therapy

Li, Q., Geng, S., Luo, H., Wang, W., Mo, Y.-Q., Luo, Q., Wang, L., Song, G.-B., Sheng, J.-P., & Xu, B. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01953-7 · Cited by 546

Mechanisms and Regulation of Cellular Senescence

Roger, L., Tomas, F., & Gire, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313173 · Cited by 395

Global consensus on optimal exercise recommendations for enhancing healthy longevity in older adults (ICFSR)

Izquierdo, M., de Souto Barreto, P., Arai, H., Bischoff-Ferrari, H. A., Cadore, E. L., Cesari, M., Chen, L.-K., Coen, P. M., Courneya, K. S., Duque, G., et al. (2025) · The Journal of nutrition, health and aging · doi:10.1016/j.jnha.2024.100401 · Cited by 273

Targeting lysosomes in human disease: from basic research to clinical applications

Cao, M., Luo, X., Wu, K., & He, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00778-y · Cited by 225

[Research progress of Adenosine 5'-monophosphate-activated protein kinase in the regulation of glycolipid metabolism].

Liu, F., Wang, Q., Qian, Y., et al. (2019) · PubMed · doi:10.13345/j.cjb.180529 · Cited by 4

Opinion: alternative views of AMP-activated protein kinase

Brenman, J. E., & Temple, B. R. S. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0005-x · Cited by 5

Down-regulation of adenosine monophosphate–activated protein kinase activity: A driver of cancer

He, X., Li, C., Ke, R., Luo, L., & Huang, D. (2017) · Tumor Biology · doi:10.1177/1010428317697576 · Cited by 19

Activation of AMP-activated protein kinase (AMPK) through inhibiting interaction with prohibitins

Kanagaki, S., Tsutsui, Y., Kobayashi, N., Komine, T., Ito, M., Akasaka, Y., Nagasawa, M., Ide, T., Omae, N., Nakao, K., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106293 · Cited by 8

Thienopyridone Drugs Are Selective Activators of AMP-Activated Protein Kinase β1-Containing Complexes

Scott, J. W., van Denderen, B. J. W., Jørgensen, S. B., Honeyman, J. E., Steinberg, G. R., Oakhill, J. S., Iseli, T. J., Koay, A. Z., Gooley, P. R., Stapleton, D., et al. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.10.005 · Cited by 262