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Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase
Open accessAbstract
The AMP-activated protein kinase (AMPK) is a critical regulator of energy balance at both the cellular and whole-body levels. Two upstream kinases have been reported to activate AMPK in cell-free assays, i.e., the tumor suppressor LKB1 and calmodulin-dependent protein kinase kinase. However, evidence that this is physiologically relevant currently only exists for LKB1. We now report that there is a significant basal activity and phosphorylation of AMPK in LKB1-deficient cells that can be stimulated by Ca2+ ionophores, and studies using the CaMKK inhibitor STO-609 and isoform-specific siRNAs show that CaMKKbeta is required for this effect. CaMKKbeta also activates AMPK much more rapidly than CaMKKalpha in cell-free assays. K(+)-induced depolarization in rat cerebrocortical slices, which increases intracellular Ca2+ without disturbing cellular adenine nucleotide levels, activates AMPK, and this is blocked by STO-609. Our results suggest a potential Ca(2+)-dependent neuroprotective pathway involving phosphorylation and activation of AMPK by CaMKKbeta.
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“Liver kinase B 1 (LKB1) [32] and calcium/calmodulin-dependent protein kinase kinase (CAMKK) 2 [33,34] can be employed as the two main mammalian upstream molecules that phosphorylate AMPK.”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [34]
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Kahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799
Self-citationOWEN, M. R., DORAN, E., & HALESTRAP, A. P. (2000) · Biochemical Journal · doi:10.1042/bj3480607 · Cited by 2,157
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
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
Self-citationLKB1 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
El-Mir, M.-Y., Nogueira, V., Fontaine, E., Avéret, N., Rigoulet, M., & Leverve, X. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.223 · Cited by 1,399
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
Self-citationThe specificities of protein kinase inhibitors: an update
BAIN, J., McLAUCHLAN, H., ELLIOTT, M., & COHEN, P. (2003) · Biochemical Journal · doi:10.1042/bj20021535 · Cited by 1,369
Self-citationHawley, 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
Self-citationThe AMP-activated protein kinase pathway – new players upstream and downstream
Hardie, D. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01540 · Cited by 1,163
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Ronnebaum, S. M., Patterson, C., & Schisler, J. C. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1180 · Cited by 39
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Tan, B., Luan, Z., Wei, X., He, Y., Wei, G., Johnstone, B. H., Farlow, M. R., & Du, Y. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.02.038 · Cited by 37
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Keller, C. W., & Lünemann, J. D. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00165 · Cited by 38
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Monteverde, T., Tait-Mulder, J., Hedley, A., Knight, J. R. P., Sansom, O. J., & Murphy, D. J. (2017) · Oncogene · doi:10.1038/onc.2017.394 · Cited by 38
Activation of AMPK by Medicinal Plants and Natural Products: Its Role in Type 2 Diabetes Mellitus
Francini, F., Schinella, G. R., & Ríos, J.-L. (2018) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557519666181128120726 · Cited by 37
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Granat, L., Hunt, R. J., & Bateman, J. M. (2020) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2019.0415 · Cited by 37
Park, S., Scheffler, T. L., & Gerrard, D. E. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.05.009 · Cited by 37
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Andris, F., & Léo, O. (2014) · International Reviews of Immunology · doi:10.3109/08830185.2014.969422 · Cited by 38
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Shen, M., Zhang, Z., Ratnam, M., & Dou, Q. P. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24494 · Cited by 37
Eom, J.-W., Lee, J., Koh, J., & Kim, Y. H. (2016) · Molecular Brain · doi:10.1186/s13041-016-0194-6 · Cited by 38
Liu, E., Corcino, Y. L., Portillo, J. C., Miao, Y., & Subauste, C. S. (2016) · Infection and Immunity · doi:10.1128/iai.00101-16 · Cited by 37
El‐Ashmawy, N. E., Khedr, N. F., El‐Bahrawy, H. A., & Mansour, H. E. A. (2017) · Tumor Biology · doi:10.1177/1010428317692235 · Cited by 38
Underwood, K. R., Tong, J., Zhu, M. J., Shen, Q. W., Means, W. J., Ford, S. P., Paisley, S. I., Hess, B. W., & Du, . (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf071573z · Cited by 37
Pham, T. H., Lee, G. H., Jin, S. W., Lee, S. Y., Han, E. H., Kim, N. D., Choi, C. Y., Jeong, G.-S., Lee, S. K., Kim, H. S., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115768 · Cited by 36
CaMKK2: bridging the gap between Ca2+ signaling and energy-sensing
McAloon, L. M., Muller, A. G., Nay, K., Lu, E. L., Smeuninx, B., Means, A. R., Febbraio, M. A., & Scott, J. W. (2024) · Essays in Biochemistry · doi:10.1042/ebc20240011 · Cited by 36
Targeting AMPK in the treatment of malignancies
Vakana, E., Altman, J. K., & Platanias, L. C. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23369 · Cited by 37
Jiang, S., Park, D. W., Gao, Y., Ravi, S., Darley-Usmar, V. M., Abraham, E., & Zmijewski, J. W. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.024 · Cited by 41
Kim, J. H., Lee, J. O., Lee, S., Moon, J. W., You, G. Y., Kim, S. J., Park, S.-H., Park, J., Lim, S. Y., Suh, P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149328 · Cited by 36
The regulation effect of AMPK in immune related diseases
Wang, J., Li, Z., Gao, L., Qi, Y., Zhu, H., & Qin, X. (2017) · Science China Life Sciences · doi:10.1007/s11427-017-9169-6 · Cited by 37
Jiang, S., Wang, Y., Luo, L., Shi, F., Zou, J., Lin, H., Ying, Y., Luo, Y., Zhan, Z., Liu, P., et al. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14279 · Cited by 36
Okubo, K., Isono, M., Asano, T., & Sato, A. (2019) · Anticancer Research · doi:10.21873/anticanres.13793 · Cited by 36
CC3/TIP30 regulates metabolic adaptation of tumor cells to glucose limitation
Chen, V., & Shtivelman, E. (2010) · Cell Cycle · doi:10.4161/cc.9.24.14230 · Cited by 36
Duong, H., Hwang, J. S., Kim, H. J., Seong, Y., & Bae, I. (2012) · International Journal of Oncology · doi:10.3892/ijo.2012.1672 · Cited by 36
Scott, J. W., Park, E., Rodriguiz, R. M., Oakhill, J. S., Issa, S. M. A., O’Brien, M. T., Dite, T. A., Langendorf, C. G., Wetsel, W. C., Means, A. R., et al. (2015) · Scientific Reports · doi:10.1038/srep14436 · Cited by 36
Bone resorption: supporting immunometabolism
van Niekerk, G., Mitchell, M., & Engelbrecht, A. (2018) · Biology Letters · doi:10.1098/rsbl.2017.0783 · Cited by 37
Ren, G., Rimando, A. M., & Mathews, S. T. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.035 · Cited by 36
Saikia, L., Talukdar, N. C., & Dutta, P. P. (2025) · Phytotherapy Research · doi:10.1002/ptr.8428 · Cited by 36
Activation of SAD Kinase by Ca2+/Calmodulin-Dependent Protein Kinase Kinase
Fujimoto, T., Yurimoto, S., Hatano, N., Nozaki, N., Sueyoshi, N., Kameshita, I., Mizutani, A., Mikoshiba, K., Kobayashi, R., & Tokumitsu, H. (2008) · Biochemistry · doi:10.1021/bi702528r · Cited by 35
Fritah, A., Steel, J. H., Parker, N., Nikolopoulou, E., Christian, M., Carling, D., & Parker, M. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032520 · Cited by 37
Targeting AMPK signaling in combating ovarian cancers: opportunities and challenges
Yung, M. M. H., Ngan, H., & Chan, D. W. (2016) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv128 · Cited by 35
Abid, H., Cartier, D., Hamieh, A., François‐Bellan, A., Bucharles, C., Pothion, H., Manecka, D.-L., Leprince, J., Adriouch, S., Boyer, O., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1352-x · Cited by 37
Wang, L., Halliday, G., Huot, J. R., Satoh, T., Baust, J., Fisher, A. J., Cook, T. G., HU, J. L., Avolio, T., Goncharov, D. A., et al. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.313883 · Cited by 37
Song, X., Tsakiridis, E. E., Steinberg, G. R., & Pei, Y. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109704 · Cited by 36
Wen, W., Chen, X., Huang, Z., Chen, D., Yu, B., He, J., Zheng, P., Luo, Y., Yan, H., & Yu, J. (2021) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2021.108750 · Cited by 37
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Zhao, Q., Song, P., & Zou, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.691585 · Cited by 37
Fyn-phosphorylated PIKE-A binds and inhibits AMPK signaling, blocking its tumor suppressive activity
Zhang, S., Qi, Q., Chan, C. B., Zhou, W., Chen, J., Luo, H. R., Appin, C., Brat, D. J., & Ye, K.-N. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.66 · Cited by 35
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 35
Morotomi‐Yano, K., Akiyama, H., & Yano, K. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.10.061 · Cited by 35
Foretz, M., Hébrard, S., Guihard, S., Leclerc, J., Cruzeiro, M. D., Hamard, G., Niedergang, F., Gaudry, M., & Viollet, B. (2010) · The FASEB Journal · doi:10.1096/fj.10-169383 · Cited by 40
AMPK in the central nervous system: physiological roles and pathological implications
Segatto, M., Rosso, P., Fioramonti, M., Fracassi, A., Marangoni, M., Taglietti, V., & Siteni, S. (2016) · Research and Reports in Biology · doi:10.2147/rrb.s90858 · Cited by 35
Tokumitsu, H., Hatano, N., Fujimoto, T., Yurimoto, S., & Kobayashi, R. (2011) · Biochemistry · doi:10.1021/bi201005g · Cited by 35
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Lim, C. T., Kola, B., Korbonits, M., & Grossman, A. B. (2010) · Progress in Brain Research · doi:10.1016/s0079-6123(10)82008-4 · Cited by 34
Peifer‐Weiß, L., Al‐Hasani, H., & Chadt, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031910 · Cited by 39
Laeger, T., Pöhland, R., Metges, C. C., & Kuhla, B. (2012) · Journal of Endocrinology · doi:10.1530/joe-11-0457 · Cited by 36
Diacylglycerol kinase-δ regulates AMPK signaling, lipid metabolism, and skeletal muscle energetics
Jiang, L. Q., Barbosa, T. D. C., Massart, J., Deshmukh, A. S., Löfgren, L., Duque-Guimaraes, D. E., Ozilgen, A., Osler, M. E., Chibalin, A., & Zierath, J. R. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00209.2015 · Cited by 35
Furno, D. L., Graziano, A. C. E., Avola, R., Giuffrida, R., Perciavalle, V., Bonina, F. P., Mannino, G., & Cardile, V. (2016) · PPAR Research · doi:10.1155/2016/4563815 · Cited by 34
AMPK allostery: A therapeutic target for the management/treatment of diabetic nephropathy
Ayinde, K. S., Olaoba, O. T., Boyenle, I. D., Du, L., Lü, Q., Yin, X., & Adelusi, T. I. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118455 · Cited by 34
Regulation of the Proteasome by AMPK in Endothelial Cells: The Role of O-GlcNAc Transferase (OGT)
Xu, J. C., Wang, S., Viollet, B., & Zou, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036717 · Cited by 34
RetractedTong, C., Peng, C. X., Wang, L., Zhang, L., Yang, X., Xu, P. A., Li, J., Delplancke, T. D. J., Zhang, H., & Qi, H. (2016) · Nutrients · doi:10.3390/nu8030138 · Cited by 34
Wang, X. J., Yang, X. P., Wang, R. X., Jiao, H., Zhao, J. P., Song, Z., & Lin, H. (2016) · Bioscience Reports · doi:10.1042/bsr20160096 · Cited by 34
Seo, H. L., Baek, S. Y., Lee, E. H., Lee, J., Lee, S., Kim, K.-Y., Jang, M., Park, M.-H., Kim, J.-H., Kim, K., et al. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.11.031 · Cited by 34
Scharf, M. T., Mackiewicz, M., Naidoo, N. N., O'Callaghan, J. P., & Pack, A. I. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05182.x · Cited by 34
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Ju, T., Lin, Y., & Chern, Y. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1025-2 · Cited by 34
AMPK-Independent LKB1 Activity Is Required for Efficient Epithelial Ovarian Cancer Metastasis
Buensuceso, A. V., Ramos-Valdes, Y., DiMattia, G. E., & Shepherd, T. G. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0530 · Cited by 35
Eduful, B. J., O’Byrne, S. N., Temme, L., Asquith, C. R. M., Liang, Y., Picado, A., Pilotte, J. R., Hossain, M. A., Wells, C. I., Zuercher, W. J., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02274 · Cited by 33
Guo, Z., Chen, X., Huang, Z., Chen, D., Li, M., Yu, B., He, J., Luo, Y., Yan, H., & Zheng, P. (2022) · Food & Function · doi:10.1039/d1fo03391c · Cited by 33
Borgquist, A., Meza, C., & Wagner, E. J. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00421.2014 · Cited by 33
Wang, X., Jia, Q., Xiao, J., Jiao, H., & Lin, H. (2015) · Stress · doi:10.3109/10253890.2015.1083551 · Cited by 33
Kenney, J. W., Sorokina, O., Genheden, M., Sorokin, A., Armstrong, J. D., & Proud, C. G. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2866-14.2015 · Cited by 33
Liu, L., & LiXian, Z. (2012) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.2012.12153 · Cited by 33
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Yamada, E., Okada, S., Bastie, C. C., Vatish, M., Nakajima, Y., Shibusawa, R., Ozawa, A., Pessin, J. E., & Yamada, M. (2016) · Oncotarget · doi:10.18632/oncotarget.11916 · Cited by 33
Moon, J.-H., Jeong, J., Hong, J., Seol, J., & Park, S. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1370-8 · Cited by 33
Zhang, N., Meng, X., Jiang, H., Ge, H., Qian, K., Zheng, Y., Park, Y., & Wang, J. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010843 · Cited by 32
BAY-3827 and SBI-0206965: Potent AMPK Inhibitors That Paradoxically Increase Thr172 Phosphorylation
Hawley, S. A., Russell, F. M., Ross, F. A., & Hardie, D. G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010453 · Cited by 32
Self-citationA chemical biology approach identifies AMPK as a modulator of melanoma oncogene MITF
Borgdorff, V., Rix, U., Winter, G. E., Gridling, M., Müller, A. C., Breitwieser, F. P., Wagner, C., Colinge, J., Bennett, K. L., Superti‐Furga, G., et al. (2013) · Oncogene · doi:10.1038/onc.2013.185 · Cited by 32
Anti-inflammatory Property of AMP-activated Protein Kinase
Noor, H. B., Mou, N. A., Salem, L., Shimul, M. F. A., Biswas, S., Akther, R., Khan, S., Raihan, S., Mohib, M. M., & Sagor, M. A. T. (2019) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/1871523018666190830100022 · Cited by 34
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Matheson, C. J., Casalvieri, K. A., Backos, D. S., Minhajuddin, M., Jordan, C. T., & Reigan, P. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112316 · Cited by 32
Li, Y., Niu, Z., Yang, J., Yang, X., Chen, Y., Li, Y., Liang, X., Zhang, J., Fan, F., Wu, P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36084-0 · Cited by 32
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Racioppi, L. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.12.004 · Cited by 32
Xu, Q., Liu, X., Zheng, X. M., Yao, Y., Wang, M., & Liu, Q. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1847 · Cited by 32
Tuerk, R. D., Thali, R. F., Auchli, Y., Rechsteiner, H., Brunisholz, R., Schlattner, U., Wallimann, T., & Neumann, D. (2007) · Journal of Proteome Research · doi:10.1021/pr070160a · Cited by 35
Thornton, C., Sardini, A., & Carling, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708987200 · Cited by 32
Revisiting the role of calcium in phagosome formation and maturation
Westman, J., Grinstein, S., & Maxson, M. E. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr1118-444r · Cited by 32
WSSV exploits AMPK to activate mTORC2 signaling for proliferation by enhancing aerobic glycolysis
Zhang, P., Fu, H.-J., Lv, L.-X., Liu, C.-F., Han, C. L., Zhao, X., & Wang, J. (2023) · Communications Biology · doi:10.1038/s42003-023-04735-z · Cited by 31
van Thuijl, H., Kola, B., & Korbonits, M. (2007) · Vitamins and hormones · doi:10.1016/s0083-6729(06)77006-6 · Cited by 31
Anti-neuroinflammatory Effect of a Novel Caffeamide Derivative, KS370G, in Microglial cells
Lu, D., Huang, B., Yeh, W., Lin, H., Huang, S., Liu, Y.-S., & Kuo, Y. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8474-y · Cited by 32
AMP-activated Protein Kinase Attenuates Nitric Oxide-induced β-Cell Death
Meares, G. P., Hughes, K. J., Jaimes, K. F., Salvatori, A., Rhodes, C. J., & Corbett, J. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047365 · Cited by 31
Insulin prevents aberrant mitochondrial phenotype in sensory neurons of type 1 diabetic rats
Aghanoori, M., Smith, D. R., Chowdhury, S. R., Sabbir, M. G., Calcutt, N. A., & Fernyhough, P. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.08.005 · Cited by 32
Wang, X., Zhou, L., Shao, L., Qian, L., Fu, X., Li, G., Luo, T., Gu, Y., Li, F., Li, J., et al. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.04.034 · Cited by 31
Abbott, M. J., Bogachus, L. D., & Turcotte, L. P. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00807.2010 · Cited by 30
Hsu, Y.-C., Meng, X., Ou, L., & Ip, M. M. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.11.011 · Cited by 30
Shen, Q., Bao, M., & Zhou, X. (2012) · Plant Signaling & Behavior · doi:10.4161/psb.20646 · Cited by 30
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Mei, H., Wang, Y., Lin, Z., & Tong, Q. (2013) · Pediatric Hematology and Oncology · doi:10.3109/08880018.2013.798058 · Cited by 30
Antonia, R. J., & Baldwin, A. S. (2018) · Science Signaling · doi:10.1126/scisignal.aan5850 · Cited by 30
Liang, Y., Tabler, T., & Dridi, S. (2020) · Frontiers in Veterinary Science · doi:10.3389/fvets.2020.544814 · Cited by 32
Chaanine, A. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910579 · Cited by 31
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Cheratta, A. R., Thayyullathil, F., Hawley, S. A., Ross, F. A., Atrih, A., Lamont, D. J., Pallichankandy, S., Subburayan, K., Alakkal, A., Rezgui, R., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110761 · Cited by 31
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Flores, K., Siqués, P., Brito, J., & Arribas, S. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116205 · Cited by 30
Mobbs, J. I., Koay, A. Z., Paolo, A. D., Bieri, M., Petrie, E. J., Gorman, M. A., Doughty, L., Parker, M. W., Stapleton, D., Griffin, M. D. W., et al. (2015) · Biochemical Journal · doi:10.1042/bj20150270 · Cited by 30
Dictyostelium, a microbial model for brain disease
Annesley, S. J., Chen, S., Francione, L. M., Sanislav, O., Chavan, A. J., Farah, C., Piazza, S. W. D., Storey, C., Ilievska, J., Fernando, S., et al. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.019 · Cited by 32
α-Lipoic acid as a triglyceride-lowering nutraceutical
Pashaj, A., Xia, M., & Moreau, R. F. (2015) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0480 · Cited by 30
Zhang, Z., Amorosa, L. F., Coyle, S. M., Macor, M., Lubitz, S. E., Carson, J. L., Birnbaum, M. J., Lee, L. Y., & Haimovich, B. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500944 · Cited by 30
Mackenzie, R., & Watt, P. (2016) · Journal of Diabetes Research · doi:10.1155/2016/6934937 · Cited by 32
Cheng, Y., Zhang, D., Zhao, L., Li, Y., Yao, X., Wang, H., Zhang, S., Liu, W., Cao, H., Yu, S., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17101695 · Cited by 30
Chen, X., Zhao, X., Lan, F., Zhou, T., Cai, H. “., Sun, H., Kong, W., & Kong, W. (2017) · Scientific Reports · doi:10.1038/s41598-017-13251-0 · Cited by 30
Wang, S., Wu, J., You, J., Shi, H., Xue, X., Huang, J., Xu, L., Jiang, G., Yuan, L., Gong, X. Q., et al. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.03.017 · Cited by 30
Wang, L., Di, L., & Noguchi, C. T. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.06.008 · Cited by 29
Popovics, P., Frigo, D. E., Schally, A. V., & Rick, F. G. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2015.1005603 · Cited by 30
Shackelford, D. B. (2013) · Journal of Carcinogenesis · doi:10.4103/1477-3163.116323 · Cited by 31
Patel, V. A., Massenburg, D., Vujicic, S., Feng, L., Tang, M., Litbarg, N. O., Antoni, A., Rauch, J., Lieberthal, W., & Levine, J. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.667345 · Cited by 32
Metadata
- Authors
- Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G.
- Affiliations
- University of Dundee (GB)
- University at Buffalo, State University of New York (US)
- Corresponding author
- Hardie, D. Grahame
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 2
- Issue
- 1
- Pages
- 9-19
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2067979493
- Cited by
- 1,589
- References
- 48
- Citations by year
- 2026: 41 · 2025: 38 · 2024: 57 · 2023: 53 · 2022: 64 · 2021: 78 · 2020: 90 · 2019: 64 · 2018: 84 · 2017: 82 · 2016: 84 · 2015: 92 · 2014: 77 · 2013: 84 · 2012: 118
- FWCI
- 27.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- AMPK, CaMKKβ, LKB1, AMPK activation, upstream kinases, calcium ionophore, STO-609, potassium depolarization, intracellular calcium, neuroprotection, energy metabolism
- MeSH terms
- Calcimycin, Acetyl-CoA Carboxylase, Adenosine Diphosphate, Adenosine Triphosphate, Animals, Benzimidazoles, Brain, Enzyme Activation, Fibroblasts, HeLa Cells, Humans, Isoquinolines, Multienzyme Complexes, Phosphoprotein Phosphatases, Phosphorylation, Substrate Specificity, Protein Serine-Threonine Kinases, RNA, Small Interfering, Mice, Rats, Naphthalimides, Calcium-Calmodulin-Dependent Protein Kinase Kinase, AMP-Activated Protein Kinases, In Vitro Techniques
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