Mechanisms of AMPK in the maintenance of ATP balance during energy metabolism

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

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

ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery

Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025

AMPK Phosphorylates and Inhibits SREBP Activity to Attenuate Hepatic Steatosis and Atherosclerosis in Diet-Induced Insulin-Resistant Mice

Li, Y., Xu, S., Mihaylova, M. M., Zheng, B., Hou, X., Jiang, B., Park, O., Luo, Z., Lefai, E., Shyy, J. Y.-J., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.009 · Cited by 1,778

The TSC1–TSC2 complex: a molecular switchboard controlling cell growth

Huang, J., & Manning, B. D. (2008) · Biochemical Journal · doi:10.1042/bj20080281 · Cited by 1,237 · cited 1×

AMPK, insulin resistance, and the metabolic syndrome

Ruderman, N. B., Carling, D., Prentki, M., & Cacicedo, J. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67227 · Cited by 873

Membrane Fatty Acid Transporters as Regulators of Lipid Metabolism: Implications for Metabolic Disease

Glatz, J. F. C., Luiken, J. J. F. P., & Bonen, A. (2010) · Physiological Reviews · doi:10.1152/physrev.00003.2009 · Cited by 751

SNF1/AMPK pathways in yeast

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

Roles of the Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR pathways in controlling growth and sensitivity to therapy-implications for cancer and aging

Steelman, L. S., Chappell, W. H., Abrams, S. L., Kempf, C. R., Long, J., Laidler, P., Mijatovic, S., Maksimovic-Ivanic, D., Stivala, F., Mazzarino, M. C., et al. (2011) · Aging · doi:10.18632/aging.100296 · Cited by 553

mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability

Mayer, C., Zhao, J., Yuan, X., & Grummt, I. (2004) · Genes & Development · doi:10.1101/gad.285504 · Cited by 505

The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.

Friesen, J. A., & Rodwell, V. W. (2004) · Genome biology · doi:10.1186/gb-2004-5-11-248 · Cited by 434

Mechanism for Fatty Acid “Sparing” Effect on Glucose-induced Transcription

Kawaguchi, T., Osatomi, K., Yamashita, H., Kabashima, T., & Uyeda, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107895200 · Cited by 423

AMPK activation increases fatty acid oxidation in skeletal muscle by activating PPARα and PGC-1

Lee, W. J., Kim, M., Park, H.-S., Kim, H. S., Jeon, M. J., Oh, K. S., Koh, E. H., Won, J. C., Kim, M.-S., Oh, G. T., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.011 · Cited by 420

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

Intracellular ATP Levels Are a Pivotal Determinant of Chemoresistance in Colon Cancer Cells

Zhou, Y., Tozzi, F., Chen, J., Fan, F., Xia, L., Wang, J., Gao, G., Zhang, A., Xia, X., Brasher, H., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-1674 · Cited by 374

Cancer stem cells: The root of tumor recurrence and metastases

Peitzsch, C., Tyutyunnykova, A., Pantel, K., & Dubrovska, A. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.02.011 · Cited by 372

Peroxisome Proliferator-activated Receptor γ Co-activator 1α (PGC-1α) and Sirtuin 1 (SIRT1) Reside in Mitochondria

Aquilano, K., Vigilanza, P., Baldelli, S., Pagliei, B., Rotilio, G., & Ciriolo, M. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070169 · Cited by 350

Thr2446 Is a Novel Mammalian Target of Rapamycin (mTOR) Phosphorylation Site Regulated by Nutrient Status

Cheng, S. W. Y., Fryer, L. G. D., Carling, D., & Shepherd, P. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300534200 · Cited by 331

Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis

Istvan, E. S., Palnitkar, M., Buchanan, S. K., & Deisenhofer, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.5.819 · Cited by 324

Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver.

Clarke, P. R., & Hardie, D. G. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07420.x · Cited by 317

Regulation of HMG-CoA reductase in mammals and yeast

Burg, J. S., & Espenshade, P. J. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.07.002 · Cited by 303

LKB1 and AMPK and the cancer-metabolism link - ten years after

Hardie, D. G., & Alessi, D. R. (2013) · BMC Biology · doi:10.1186/1741-7007-11-36 · Cited by 301

Metformin Induces Apoptosis and Cell Cycle Arrest Mediated by Oxidative Stress, AMPK and FOXO3a in MCF-7 Breast Cancer Cells

Queiroz, E. A. I. F., Puukila, S., Eichler, R., Sampaio, S. C., Forsyth, H. L., Lees, S. J., Barbosa, A. M., Dekker, R. F. H., Fortes, Z. B., & Khaper, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098207 · Cited by 278

Effects of α‐AMPK knockout on exercise‐induced gene activation in mouse skeletal muscle

Jørgensen, S. B., Wojtaszewski, J. F. P., Viollet, B., Andreelli, F., Birk, J. B., Hellsten, Y., Schjerling, P., Vaulont, S., Neufer, P. D., Richter, E. A., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3144fje · Cited by 274

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

Phosphorylation of ULK1 by AMPK regulates translocation of ULK1 to mitochondria and mitophagy

Tian, W., Li, W., Chen, Y., Yan, Z., Huang, X., Zhuang, H., Zhong, W., Chen, Y., Wu, W., Lin, C., et al. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.020 · Cited by 199

Transcriptional Regulation of Pyruvate Dehydrogenase Kinase

Jeong, J. Y., Jeoung, N. H., Park, K.-G., & Lee, I.-K. (2012) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2012.36.5.328 · Cited by 179

Inhibition of lung cancer growth: ATP citrate lyase knockdown and statin treatment leads to dual blockade of mitogen‐activated protein Kinase (MAPK) and Phosphatidylinositol‐3‐kinase (PI3K)/AKT pathways

Hanai, J., Doro, N., Sasaki, A. T., Kobayashi, S., Cantley, L. C., Seth, P., & Sukhatme, V. P. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.22895 · Cited by 165

Role of AMPK-mediated adaptive responses in human cells with mitochondrial dysfunction to oxidative stress

Wu, S., Wu, Y., Wu, T.-P., & Wei, Y. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.034 · Cited by 165

CTRP1 Protein Enhances Fatty Acid Oxidation via AMP-activated Protein Kinase (AMPK) Activation and Acetyl-CoA Carboxylase (ACC) Inhibition

Peterson, J. M., Aja, S. M., Wei, Z., & Wong, G. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.278333 · Cited by 158

AMPK → ULK1 → Autophagy

Roach, P. J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05565-11 · Cited by 157

AMPK phosphorylation of ACC2 is required for skeletal muscle fatty acid oxidation and insulin sensitivity in mice

O’Neill, H. M., Lally, J., Galić, S., Thomas, M. M., Azizi, P. D., Fullerton, M. D., Smith, B. K., Pulinilkunnil, T., Chen, Z., Samaan, M. C., et al. (2014) · Diabetologia · doi:10.1007/s00125-014-3273-1 · Cited by 154

AMPK Enhances Insulin-Stimulated GLUT4 Regulation via Lowering Membrane Cholesterol

Habegger, K. M., Hoffman, N. J., Ridenour, C. M., Brozinick, J. T., & Elmendorf, J. S. (2012) · Endocrinology · doi:10.1210/en.2011-2099 · Cited by 152

Extracellular ATP is internalized by macropinocytosis and induces intracellular ATP increase and drug resistance in cancer cells

Qian, Y., Wang, X., Liu, Y., Li, Y., Colvin, R. A., Tong, L., Wu, S., & Chen, X. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.06.008 · Cited by 149

Oxidative stress activates AMPK in cultured cells primarily by increasing cellular AMP and/or ADP

Auciello, F. R., Ross, F. A., Ikematsu, N., & Hardie, D. G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.07.025 · Cited by 138

Targeting the Phosphatidylinositol 3-Kinase/Akt/Mammalian Target of Rapamycin Signaling Network in Cancer Stem Cells

Martelli, A. M., Evangelisti, C., Follo, M., Ramazzotti, G., Fini, M., Giardino, R., Manzoli, L., McCubrey, J. A., & Cocco, L. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796011201 · Cited by 116

CD36‐dependent signaling mediates fatty acid‐induced gut release of secretin and cholecystokinin

Sundaresan, S., Shahid, R. A., Riehl, T. E., Chandra, R., Nassir, F., Stenson, W. F., Liddle, R. A., & Abumrad, N. A. (2012) · The FASEB Journal · doi:10.1096/fj.12-217703 · Cited by 112

Extracellular ATP a New Player in Cancer Metabolism: NSCLC Cells Internalize ATP In Vitro and In Vivo Using Multiple Endocytic Mechanisms

Qian, Y., Wang, X., Li, Y., Cao, Y., & Chen, X. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0118 · Cited by 108

Adenosine Monophosphate (AMP)-Activated Protein Kinase: A New Target for Nutraceutical Compounds

Marín‐Aguilar, F., Pavillard, L. E., Giampieri, F., Bullón, P., & Cordero, M. D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020288 · Cited by 105

In Vivo, Fatty Acid Translocase (CD36) Critically Regulates Skeletal Muscle Fuel Selection, Exercise Performance, and Training-induced Adaptation of Fatty Acid Oxidation

McFarlan, J. T., Yoshida, Y., Jain, S. S., Han, X.-X., Snook, L. A., Lally, J., Smith, B. K., Glatz, J. F. C., Luiken, J. J. F. P., Sayer, R. A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315358 · Cited by 103

ATP citrate lyase knockdown impacts cancer stem cells in vitro

Hanai, J.-I., Doro, N. C., Seth, P., & Sukhatme, V. P. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.215 · Cited by 102

Activation of AMPK is essential for AICAR-induced glucose uptake by skeletal muscle but not adipocytes

Sakoda, H., Ogihara, T., Anai, M., Fujishiro, M., Ono, H., Onishi, Y., Katagiri, H., Abe, M., Fukushima, Y., Shojima, N., et al. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00455.2001 · Cited by 96

Identification of the Citrate-binding Site of Human ATP-Citrate Lyase Using X-ray Crystallography

Sun, T., Hayakawa, K., Bateman, K., & Fraser, M. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.078667 · Cited by 96

Adiponectin promotes pancreatic cancer progression by inhibiting apoptosis via the activation of AMPK/Sirt1/PGC-1α signaling

Huang, B., Cheng, X., Wang, D., Peng, M., Xue, Z., Da, Y., Zhang, N., Yao, Z., Li, M., Xu, A., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.1963 · Cited by 92

AMPK-α1 functions downstream of oxidative stress to mediate neuronal atrophy in Huntington's disease

Ju, T., Chen, H., Chen, Y., Chang, C., Chang, C., & Chern, Y. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.012 · Cited by 90

ChREBP, a glucose-responsive transcriptional factor, enhances glucose metabolism to support biosynthesis in human cytomegalovirus-infected cells

Yu, Y., Maguire, T. G., & Alwine, J. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310779111 · Cited by 83

ATP promotes cell survival via regulation of cytosolic [Ca2+] and Bcl-2/Bax ratio in lung cancer cells

Song, S., Jacobson, K., McDermott, K. M., Reddy, S. P., Cress, A. E., Tang, H., Dudek, S. M., Black, S. M., Garcia, J. G. N., Makino, A., et al. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00092.2015 · Cited by 81

STIM1 regulates calcium signaling in taste bud cells and preference for fat in mice

Dramane, G., Abdoul‐Azize, S., Hichami, A., Vögtle, T., Akpona, S., Chouabe, C., Sadou, H., Nieswandt, B., Besnard, P., & Khan, N. A. (2012) · Journal of Clinical Investigation · doi:10.1172/jci59953 · Cited by 80

Oxidative stress induces phosphorylation of neuronal NOS in cardiomyocytes through AMP-activated protein kinase (AMPK)

Kar, R., Kellogg, D. L., & Roman, L. J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.113 · Cited by 75

The Glucose Sensor ChREBP Links De Novo Lipogenesis to PPARγ Activity and Adipocyte Differentiation

Witte, N., Muenzner, M., Rietscher, J., Knauer, M., Heidenreich, S., Nuotio-Antar, A. M., Graef, F. A., Fedders, R., Tolkachov, A., Göhring, I., et al. (2015) · Endocrinology · doi:10.1210/en.2015-1209 · Cited by 72

Transcriptional activation of hypoxia‐inducible factor‐1α by HDAC4 and HDAC5 involves differential recruitment of p300 and FIH‐1

Seo, H., Kim, E., Na, H., & Lee, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.11.044 · Cited by 71

Salicylate improves macrophage cholesterol homeostasis via activation of Ampk

Fullerton, M. D., Ford, R. J., McGregor, C., LeBlond, N. D., Snider, S. A., Stypa, S., Day, E. A., Lhoták, Š., Schertzer, J. D., Austin, R. C., et al. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m058875 · Cited by 70

Extracellular ATP reduces tumor sphere growth and cancer stem cell population in glioblastoma cells

Ledur, P. F., Villodre, E. S., Paulus, R., Cruz, L. A., Flores, D. G., & Lenz, G. (2011) · Purinergic Signalling · doi:10.1007/s11302-011-9252-9 · Cited by 66

Dietary fat intake and cancer risk: a controversial and instructive story

Willett, W. C. (1998) · Seminars in Cancer Biology · doi:10.1006/scbi.1998.0076 · Cited by 55

Extracellular ATP enhances in vitro invasion of prostate cancer cells by activating Rho GTPase and upregulating MMPs expression

Zhang, Y., Gong, L. H., Zhang, H., Du, Q., You, J., Tian, X., & Fang, W. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.01.010 · Cited by 53

Prognostic Value of Malic Enzyme and ATP-Citrate Lyase in Non-Small Cell Lung Cancer of the Young and the Elderly

Csanádi, Á., Kayser, C., Donauer, M., Gumpp, V., Aumann, K., Rawluk, J. K., Prasse, A., Hausen, A. Z., Wiesemann, S. D., Werner, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126357 · Cited by 44

The androgen derivative 5α-androstane-3β,17β-diol inhibits tumor necrosis factor α and lipopolysaccharide induced inflammatory response in human endothelial cells and in mice aorta

Norata, G. D., Cattaneo, P., Poletti, A., & Catapano, A. L. (2010) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2010.05.015 · Cited by 44

Visfatin, a novel adipokine, stimulates glucose uptake through the Ca2+-dependent AMPK–p38 MAPK pathway in C2C12 skeletal muscle cells

Lee, J. O., Kim, N., Lee, H., Lee, Y. W., Kim, J. K., Kim, H. I., Lee, S., Kim, S. J., Park, S. H., & Kim, H. S. (2015) · Journal of Molecular Endocrinology · doi:10.1530/jme-14-0274 · Cited by 37

MEF2A Binding to the Glut4 Promoter Occurs via an AMPKα2-Dependent Mechanism

Gong, H., XIE, J., Zhang, N., Lu, Y., & Zhang, Y. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31820f6093 · Cited by 34

HIF-1 suppresses lipid catabolism to promote cancer progression

Zhang, H. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.980184 · Cited by 31

ChREBP binding and histone modifications modulate hepatic expression of the Fasn gene in a metabolic syndrome rat model

Suzuki, T., Muramatsu, T., Morioka, K., Goda, T., & Mochizuki, K. (2015) · Nutrition · doi:10.1016/j.nut.2015.01.005 · Cited by 30

Low glucose stress decreases cellular NADH and mitochondrial ATP in colonic epithelial cancer cells: Influence of mitochondrial substrates

Circu, M. L., Maloney, R. E., & Aw, T. Y. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.01.001 · Cited by 27

AMPK, a metabolic sensor, is involved in isoeugenol-induced glucose uptake in muscle cells

Kim, N., Lee, J. O., Lee, H., Lee, Y. W., Kim, H. I., Kim, S. J., Park, S. H., Lee, C. S., Ryoo, S. W., Hwang, G., et al. (2015) · Journal of Endocrinology · doi:10.1530/joe-15-0302 · Cited by 22

Skeletal muscle fatty acid oxidation is not directly associated with AMPK or ACC2 phosphorylation

Alkhateeb, H. H., Holloway, G. P., & Bonen, A. (2011) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h11-024 · Cited by 11

Response to energy depletion: miR-451/AMPK loop

Bronisz, A., Chiocca, E. A., & Godlewski, J. A. (2015) · Oncotarget · doi:10.18632/oncotarget.4606 · Cited by 7

Semaglutide attenuates excessive exercise-induced myocardial injury through inhibiting oxidative stress and inflammation in rats

Li, Q., Tuo, X., Li, B., Deng, Z., Qiu, Y., & Xie, H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117531 · Cited by 72

Oxytocin may have a therapeutical potential against cardiovascular disease. Possible pharmaceutical and behavioral approaches

Buemann, B., & Uvnäs-Moberg, K. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.109597 · Cited by 66

Insulin Regulation of Hepatic Lipid Homeostasis

Uehara, K., Santoleri, D., Whitlock, A. E. G., & Titchenell, P. M. (2023) · Comprehensive Physiology · doi:10.1002/cphy.c220015 · Cited by 49

Ameliorating the hallmarks of cellular senescence in skeletal muscle myogenic progenitors in vitro and in vivo

Shahini, A., Rajabian, N., Choudhury, D., Shahini, S., Vydiam, K., Nguyen, T., Kulczyk, J., Santarelli, T., Ikhapoh, I., Zhang, Y., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe5671 · Cited by 38

Nucleoside diphosphate kinases 1 and 2 regulate a protective liver response to a high-fat diet

Iuso, D., Garcia-Saez, I., Couté, Y., Yamaryo-Botté, Y., Boeri Erba, E., Adrait, A., Zeaiter, N., Tokarska-Schlattner, M., Jilkova, Z. M., Boussouar, F., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh0140 · Cited by 14