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Defining the Mechanism of Activation of AMP-activated Protein Kinase by the Small Molecule A-769662, a Member of the Thienopyridone Family
Open accessAbstract
AMP-activated protein kinase (AMPK) plays a key role in maintaining energy homeostasis. Activation of AMPK in peripheral tissues has been shown to alleviate the symptoms of metabolic diseases, such as type 2 diabetes, and consequently AMPK is a target for treatment of these diseases. Recently, a small molecule activator (A-769662) of AMPK was identified that had beneficial effects on metabolism in ob/ob mice. Here we show that A-769662 activates AMPK both allosterically and by inhibiting dephosphorylation of AMPK on Thr-172, similar to the effects of AMP. A-769662 activates AMPK harboring a mutation in the gamma subunit that abolishes activation by AMP. An AMPK complex lacking the glycogen binding domain of the beta subunit abolishes the allosteric effect of A-769662 but not the allosteric activation by AMP. Moreover, mutation of serine 108 to alanine, an autophosphorylation site within the glycogen binding domain of the beta1 subunit, almost completely abolishes activation of AMPK by A-769662 in cells and in vitro, while only partially reducing activation by AMP. Based on our results we propose a model for activation of AMPK by A-769662. Importantly, this model may provide clues for understanding the mechanism by which AMP leads to activation of AMPK, which in turn may help in the identification of other AMPK activators.
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“Activation loop phosphorylation increases AMPK activity by about 100-fold, while allosteric regulation changes AMPK activity up to tenfold in mammalian cells and about twofold in recombinant, bacterially produced AMPK [26,28,38,39].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [38]
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Cites
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
Self-citationKahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799
Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053
Self-citationThe Kinase LKB1 Mediates Glucose Homeostasis in Liver and Therapeutic Effects of Metformin
Shaw, R. J., Lamia, K. A., Vasquez, D., Koo, S.-H., Bardeesy, N., DePinho, R. A., Montminy, M., & Cantley, L. C. (2005) · Science · doi:10.1126/science.1120781 · Cited by 1,950
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
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
Self-citationAMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus
Minokoshi, Y., Alquier, T., Furukawa, N., Kim, Y.-B., Lee, A., Xue, B., Mu, J., Foufelle, F., Ferré, P., Birnbaum, M. J., et al. (2004) · Nature · doi:10.1038/nature02440 · Cited by 1,637
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
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
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Zhang, J., Yang, P. L., & Gray, N. S. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2559 · Cited by 2,648
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Garcia, D., & Shaw, R. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.032 · Cited by 2,061
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Lin, S., & Hardie, D. G. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.009 · Cited by 1,198
AMPK: An Emerging Drug Target for Diabetes and the Metabolic Syndrome
Zhang, B. B., Zhou, G., & Li, C. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.012 · Cited by 1,042
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
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 886
AMPK activators: mechanisms of action and physiological activities
Kim, J., Yang, G., Kim, Y., Kim, J., & Ha, J. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.16 · Cited by 817
AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control
González, A., Hall, M. N., Lin, S.-C., & Hardie, D. G. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.015 · Cited by 797
Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation
Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773
AMP-activated protein kinase: the current landscape for drug development
Steinberg, G. R., & Carling, D. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0019-2 · Cited by 785
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
AMPK signalling in health and disease
Carling, D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.01.005 · Cited by 797
AMPK—Sensing Energy while Talking to Other Signaling Pathways
Hardie, D. G. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.09.013 · Cited by 597
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
AMPK: a metabolic gauge regulating whole-body energy homeostasis
Lage, R., Diéguez, C., Vidal‐Puig, A., & López, M. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.09.007 · Cited by 512
Treatment of nonalcoholic fatty liver disease: role of AMPK
Smith, B. K., Marcinko, K., Desjardins, E. M., Lally, J., Ford, R. J., & Steinberg, G. R. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00225.2016 · Cited by 509
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
AMPK: positive and negative regulation, and its role in whole-body energy homeostasis
Hardie, D. G. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.09.004 · Cited by 485
Molecular mechanism of action of metformin: old or new insights?
Rena, G., Pearson, E. R., & Sakamoto, K. (2013) · Diabetologia · doi:10.1007/s00125-013-2991-0 · Cited by 479
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McBride, A., Ghilagaber, S., Nikolaev, A., & Hardie, D. G. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.11.008 · Cited by 432
AMPK activation: a therapeutic target for type 2 diabetes?
Saha, A. K., Coughlan, K. A., Valentine, R. J., & Ruderman, N. B. (2014) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s43731 · Cited by 458
MicroRNA-451 Regulates LKB1/AMPK Signaling and Allows Adaptation to Metabolic Stress in Glioma Cells
Godlewski, J. A., Nowicki, M. O., Bronisz, A., Nuovo, G. J., Palatini, J., Lay, M. D. D., Brocklyn, J. R. V., Ostrowski, M. C., Chiocca, E. A., & Lawler, S. E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.018 · Cited by 426
AMP-activated protein kinase: nature's energy sensor
Carling, D., Mayer, F. V., Sanders, M. J., & Gamblin, S. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.610 · Cited by 387
Important role of the LKB1-AMPK pathway in suppressing tumorigenesis in PTEN-deficient mice
Huang, X., Wullschleger, S., Shpiro, N., McGuire, V. A., Sakamoto, K., Woods, Y. L., Mcburnie, W., Fleming, S., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20080557 · Cited by 396
AMP-activated protein kinase: new regulation, new roles?
Carling, D., Thornton, C., Woods, A., & Sanders, M. J. (2012) · Biochemical Journal · doi:10.1042/bj20120546 · Cited by 390
AMP-Activated Protein Kinase: A Target for Drugs both Ancient and Modern
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Lanna, A., Henson, S. M., Escors, D., & Akbar, A. N. (2014) · Nature Immunology · doi:10.1038/ni.2981 · Cited by 328
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Wang, Q., Liu, S., Zhai, A., Zhang, B., & Tian, G. (2018) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00724 · Cited by 324
AMPK: Lessons from transgenic and knockout animals
Viollet, B. (2009) · Frontiers in bioscience · doi:10.2741/3229 · Cited by 314
Srivastava, R. A. K., Pinkosky, S. L., Filippov, S. I., Hanselman, J. C., Cramer, C. T., & Newton, R. S. (2012) · Journal of Lipid Research · doi:10.1194/jlr.r025882 · Cited by 308
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Zadra, G., Photopoulos, C., & Loda, M. F. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.03.010 · Cited by 301
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Hardie, D. G., & Ashford, M. L. J. (2014) · Physiology · doi:10.1152/physiol.00050.2013 · Cited by 280
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Wu, L., Zhang, L., Li, B., Jiang, H., Duan, Y., Xie, Z., Shuai, L., Li, J., & Li, J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00122 · Cited by 255
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Yan, Y., Zhou, X. E., Xu, H. E., & Melcher, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113534 · Cited by 254
AMPK signaling and its targeting in cancer progression and treatment
Hsu, C.-C., Peng, D., Cai, Z., & Lin, H. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.04.006 · Cited by 265
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
Witczak, C. A., Sharoff, C. G., & Goodyear, L. J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8244-6 · Cited by 253
Energy status dictates PD-L1 protein abundance and anti-tumor immunity to enable checkpoint blockade
Dai, X., Bu, X., Gao, Y., Guo, J., Hu, J., Jiang, C., Zhang, Z., Xu, K., Duan, J., He, S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.037 · Cited by 257
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Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis
Banko, M. R., Allen, J. J., Schaffer, B. E., Wilker, E., Tsou, P., White, J. L., Villén, J., Wang, B., Kim, S. R., Sakamoto, K., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.11.005 · Cited by 252
Christopoulos, A., Changeux, J., Catterall, W. A., Fabbro, D., Burris, T. P., Cidlowski, J. A., Olsen, R. W., Peters, J. A., Neubig, R. R., Pin, J., et al. (2014) · Pharmacological Reviews · doi:10.1124/pr.114.008862 · Cited by 246
Discrete mechanisms of mTOR and cell cycle regulation by AMPK agonists independent of AMPK
Liu, X., Chhipa, R. R., Pooya, S., Wortman, M. D., Yachyshin, S., Chow, L. M. L., Kumar, A., Zhou, X., Sun, Y. H., Quinn, B., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311121111 · Cited by 232
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Zorn, J. A., & Wells, J. A. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.318 · Cited by 222
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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
Salt, I. P., & Hardie, D. G. (2017) · Circulation Research · doi:10.1161/circresaha.117.309633 · Cited by 190
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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
Metabolic alterations and targeted therapies in prostate cancer
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Hardie, D. G. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390001 · Cited by 180
Regulation of AMP-activated protein kinase by natural and synthetic activators
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Kim, A. S., Miller, E. J., Wright, T. M., Li, J., Qi, D., Atsina, K. B.-T., Zaha, V. G., Sakamoto, K., & Young, L. H. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.03.003 · Cited by 176
Gusdon, A. M., Song, K., & Qu, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/637027 · Cited by 172
Mitochondrial respiratory chain deficiency inhibits lysosomal hydrolysis
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The LKB1-salt-inducible kinase pathway functions as a key gluconeogenic suppressor in the liver
Patel, K., Foretz, M., Marion, A., Campbell, D. G., Gourlay, R., Boudaba, N., Tournier, E., Titchenell, P. M., Peggie, M. W., Deák, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5535 · Cited by 171
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
Small Molecule Antagonizes Autoinhibition and Activates AMP-activated Protein Kinase in Cells
Pang, T., Zhang, Z., Gu, M., Qiu, B., Yu, L.-F., Cao, P.-R., Shao, W., Su, M., Li, J.-Y., Nan, F., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710114200 · Cited by 159
Hunter, R. W., Treebak, J. T., Wojtaszewski, J. F. P., & Sakamoto, K. (2011) · Diabetes · doi:10.2337/db10-1148 · Cited by 151
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Omar, B. A., Zmuda‐Trzebiatowska, E., Manganiello, V. C., Göransson, O., & Degerman, E. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.015 · Cited by 141
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Fabbro, D. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.095489 · Cited by 141
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Vara‐Ciruelos, D., Russell, F. M., & Hardie, D. G. (2019) · Open Biology · doi:10.1098/rsob.190099 · Cited by 140
Important role for AMPKαl in limiting skeletal muscle cell hypertrophy
Mounier, R., Lantier, L., Leclerc, J., Sotiropoulos, A., Pende, M., Daegelen, D., Sakamoto, K., Foretz, M., & Viollet, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-119057 · 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
Targeting Cancer with Small-Molecular-Weight Kinase Inhibitors
Fabbro, D., Cowan‐Jacob, S. W., Möbitz, H., & Martiny‐Baron, G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-337-0_1 · Cited by 130
Autophagy in health and disease: From molecular mechanisms to therapeutic target
Lu, G. X., Wang, Y., Shi, Y. P., Zhang, Z., Huang, C., He, W., Wang, C., & Shen, H. (2022) · MedComm · doi:10.1002/mco2.150 · Cited by 135
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Paiva, M. S. A., Rutter‐Locher, Z., Gonçalves, L. M. M., Providência, L. A., Davidson, S. M., Yellon, D. M., & Mocanu, M. M. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00707.2010 · Cited by 122
AMP activated protein kinase: a next generation target for total metabolic control
Misra, P. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.1.91 · Cited by 117
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Esteve‐Puig, R., Canals, F., Colomé, N., Merlino, G. T., & Recio, J. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004771 · Cited by 114
Madhavi, Y. V., Gaikwad, N. B., Yerra, V. G., Kalvala, A. K., Nanduri, S., & Kumar, A. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180406120051 · Cited by 117
Structure of an AMPK complex in an inactive, ATP-bound state
Yan, Y., Mukherjee, S., Harikumar, K. G., Strutzenberg, T. S., Zhou, X. E., Suino-Powell, K. M., Xu, T.-H., Sheldon, R. D., Lamp, J. A., Brunzelle, J. S., et al. (2021) · Science · doi:10.1126/science.abe7565 · Cited by 114
Effects of metformin on breast cancer cell proliferation, the AMPK pathway and the cell cycle
Hadad, S. M., Hardie, D. G., Appleyard, V., & Thompson, A. M. (2013) · Clinical & Translational Oncology · doi:10.1007/s12094-013-1144-8 · Cited by 113
Ewart, M., & Kennedy, S. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.11.002 · Cited by 112
Treebak, J. T., Birk, J. B., Hansen, B. F., Olsen, G. S., & Wojtaszewski, J. F. P. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00051.2009 · Cited by 112
Ppm1E is an in cellulo AMP-activated protein kinase phosphatase
Voß, M., Paterson, J., Kelsall, I. R., Martín‐Granados, C., Hastie, C. J., Peggie, M. W., & Cohen, P. T. W. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.08.010 · Cited by 111
Lee, K., Hsu, E., Guh, J., Yang, M., Wang, D.-S., Kulp, S. K., Shapiro, C. L., & Chen, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264598 · Cited by 106
Vázquez‐Martín, A., Vellón, L., Quirós, P. M., Cufí, S., de Galarreta, E. R., Oliveras‐Ferraros, C., Martín, Á. G., Martı́n-Castillo, B., López-Otı́n, C., & Menéndez, J. A. (2012) · Cell Cycle · doi:10.4161/cc.11.5.19450 · Cited by 98
Lai, Y., Kviklyte, S., Vertommen, D., Lantier, L., Foretz, M., Viollet, B., Hallén, S., & Rider, M. H. (2014) · Biochemical Journal · doi:10.1042/bj20131673 · Cited by 102
Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism
Pelosse, M., Cottet‐Rousselle, C., Bidan, C. M., Dupont, A., Gupta, K., Berger, I., & Schlattner, U. (2019) · Nature Communications · doi:10.1038/s41467-019-08938-z · Cited by 99
Moreno-Andrés, D., Knecht, E., Viollet, B., & Sanz, P. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.044 · Cited by 95
The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs
Dite, T. A., Ling, N. X. Y., Scott, J. W., Hoque, A., Galić, S., Parker, B. L., Ngoei, K. R. W., Langendorf, C. G., O’Brien, M. T., Kundu, M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00628-y · Cited by 96
Hypothalamic AMP-activated protein kinase as a mediator of whole body energy balance
de Morentin, P. B. M., González, C. R., Saha, A. K., Martins, L., Diéguez, C., Vidal‐Puig, A., Tena‐Sempere, M., & López, M. (2011) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-011-9165-5 · Cited by 96
Langendorf, C. G., Ngoei, K. R. W., Scott, J. W., Ling, N. X. Y., Issa, S. M. A., Gorman, M. A., Parker, M. W., Sakamoto, K., Oakhill, J. S., & Kemp, B. E. (2016) · Nature Communications · doi:10.1038/ncomms10912 · Cited by 94
Structural Properties of AMP-activated Protein Kinase
Riek, U., Scholz, R., Konarev, P. V., Rufer, A. C., Suter, M., Nazabal, A., Ringler, P., Chami, M., Müller, S. A., Neumann, D., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708379200 · Cited by 93
Inhibition of AMP kinase by the protein phosphatase 2a heterotrimer, PP2APpp2r2d
Joseph, B. K., Liu, H.-Y., Francisco, J., Pandya, D., Donigan, M., Gallo-Ebert, C., Giordano, C., Bata, A., & Nickels, J. T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.626259 · Cited by 91
Hall, D. T., Griss, T., Ma, J. F., Sanchez, B. J., Sadek, J., Tremblay, A. M. K., Mubaid, S., Omer, A., Ford, R. J., Bedard, N., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708307 · Cited by 88
AMP-activated protein kinase – not just an energy sensor
Hardie, D. G., & Lin, S. (2017) · F1000Research · doi:10.12688/f1000research.11960.1 · Cited by 91
Recent and emerging anti‐diabetes targets
Mohler, M. L., He, Y., Wu, Z., Hwang, D., & Miller, D. D. (2008) · Medicinal Research Reviews · doi:10.1002/med.20142 · Cited by 88
Beyond AICA riboside: In search of new specific AMP‐activated protein kinase activators
Guigas, B., Sakamoto, K., Taleux, N., Reyna, S. M., Musi, N., Viollet, B., & Hue, L. (2009) · IUBMB Life · doi:10.1002/iub.135 · Cited by 86
Hutchinson, D. S., Summers, R. J., & Bengtsson, T. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.05.008 · Cited by 88
Promise and challenges for direct small molecule AMPK activators
Olivier, S., Foretz, M., & Viollet, B. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.049 · Cited by 90
Metadata
- Authors
- Sanders, M. J., Ali, Z. S., Hegarty, B. D., Heath, R., Snowden, M. A., & Carling, D.
- Affiliations
- Hammersmith Hospital (GB)
- GlaxoSmithKline (United Kingdom) (GB)
- Corresponding author
- Carling, David
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-11
- Volume
- 282
- Issue
- 45
- Pages
- 32539-32548
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2085558309
- Cited by
- 347
- References
- 47
- Citations by year
- 2026: 12 · 2025: 7 · 2024: 6 · 2023: 11 · 2022: 13 · 2021: 20 · 2020: 18 · 2019: 14 · 2018: 31 · 2017: 21 · 2016: 28 · 2015: 19 · 2014: 40 · 2013: 23 · 2012: 16
- FWCI
- 6.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- AMPK, A769662, allosteric activation, energy homeostasis, type 2 diabetes, ob/ob mice
- MeSH terms
- Biphenyl Compounds, Cell Line, Enzyme Activation, Humans, Multienzyme Complexes, Mutation, Phosphorylation, Protein Binding, Pyridines, Pyrones, Thiophenes, Threonine, Protein Serine-Threonine Kinases, Protein Subunits, AMP-Activated Protein Kinases
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