The DOI matches its Crossref record; 226 of the 226 references it cites were found in a registry or an index.
AMPK inhibition in health and disease
Open accessAbstract
All living organisms depend on dynamic mechanisms that repeatedly reassess the status of amassed energy, in order to adapt energy supply to demand. The AMP-activated protein kinase (AMPK) alphabetagamma heterotrimer has emerged as an important integrator of signals managing energy balance. Control of AMPK activity involves allosteric AMP and ATP regulation, auto-inhibitory features and phosphorylation of its catalytic (alpha) and regulatory (beta and gamma) subunits. AMPK has a prominent role not only as a peripheral sensor but also in the central nervous system as a multifunctional metabolic regulator. AMPK represents an ideal second messenger for reporting cellular energy state. For this reason, activated AMPK acts as a protective response to energy stress in numerous systems. However, AMPK inhibition also actively participates in the control of whole body energy homeostasis. In this review, we discuss recent findings that support the role and function of AMPK inhibition under physiological and pathological states.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“It comprises three sub-units, each of which have multiple isoforms and confer tissue specificity (549).”
From Placental Origins of Chronic Disease (2016) · cites this paper as [549]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
5 retracted
Activation of the AMP-activated Protein Kinase by the Anti-diabetic Drug Metformin in Vivo
Zou, M., Kirkpatrick, S. S., Davis, B. J., Nelson, J. S., Wiles, W. G., Schlattner, U., Neumann, D., Brownlee, M., Freeman, M. B., & Goldman, M. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404421200 · Cited by 480
RetractedActivation of Protein Phosphatase 2A by Palmitate Inhibits AMP-activated Protein Kinase
Wu, Y., Song, P., Xu, J., Zhang, M., & Zou, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608310200 · Cited by 283
RetractedRopelle, E. R., Pauli, J. R., Fernandes, M. F., Rocco, S. A., Marin, R. M., Morari, J., Souza, K. K., Dias, M. M., Gomes‐Marcondes, M. C. C., Gontijo, J. A. R., et al. (2007) · Diabetes · doi:10.2337/db07-0573 · Cited by 214
RetractedDual Role of Interleukin-6 in Regulating Insulin Sensitivity in Murine Skeletal Muscle
Nieto-Vazquez, I., Fernández-Veledo, S., de Alvaro, C., & Lorenzo, M. (2008) · Diabetes · doi:10.2337/db07-1062 · Cited by 209
RetractedWang, S., Xu, J. C., Song, P., Viollet, B., & Zou, M. (2009) · Diabetes · doi:10.2337/db09-0267 · Cited by 137
Self-citationRetractedUnderstanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197
Xu, H., Barnes, G. T., Yang, Q., Tan, G., Yang, D., Chou, C. J., Sole, J., Nichols, A., Ross, J. S., Tartaglia, L. A., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319451 · Cited by 6,760
TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
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
Randle, P. J., Garland, P. B., Hales, C. N., & Newsholme, E. A. (1963) · The Lancet · doi:10.1016/s0140-6736(63)91500-9 · Cited by 5,093
Research works printed but not linked: 18
- Arad M, 2002, J Clin Invest, 109, 357, 10.1172/JCI0214571 · DOI
- Bai A, 2010, J Pharmacol Exp Ther. (in press).
- Billaud M, 2008, Metformin: Mechanistic Insights Towards New Applications
- Bradley EA, 2010, Arterioscler Thromb Vasc Biol 30: 1137-1142.
- Brochu M, 2001, J Clin Endocrinol Metab, 86, 1020
- Fogarty S, 2009, Biochim Biophys Acta 1804: 581-591.
- 10.1152/ajpregu.90971.2008 · DOI
- Lee JH, 2007, Nature 447:1017-1020.
- Lopaschuk GD, 1990, Circ Res, 66, 546, 10.1161/01.RES.66.2.546 · DOI
- Muse ED, 2004, J Clin Invest, 114, 232, 10.1172/JCI200421270 · DOI
- Olson DP, 2010, Proc Natl Acad Sci USA.
- Osuka K, 2009, J Neurotrauma 26: 1157-1165
- Proud CG, 1997, Biochem J, 328, 329, 10.1042/bj3280329 · DOI
- 10.1042/bj3340177 · DOI
- 10.1042/bj3350533 · DOI
- Scott JW, 2004, J Clin Invest, 113, 274, 10.1172/JCI19874 · DOI · Paper page
- Viollet B, 2003, J Clin Invest, 111, 91, 10.1172/JCI16567 · DOI · Paper page
- Viollet B, 2003, J Clin Invest, 111, 91, 10.1172/JCI16567 · DOI · Paper page
Cited by
Sorted by citations
AMP-Activated Protein Kinase (AMPK) Controls the Aging Process via an Integrated Signaling Network
Salminen, A., & Kaarniranta, K. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2011.12.005 · Cited by 860
Placental Origins of Chronic Disease
Burton, G. J., Fowden, A. L., & Thornburg, K. L. (2016) · Physiological Reviews · doi:10.1152/physrev.00029.2015 · Cited by 717
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
Pinkosky, S. L., Newton, R. S., Day, E. A., Ford, R. J., Lhotak, S., Austin, R. C., Birch, C. M., Smith, B. K., Filippov, S., Groot, P. H. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13457 · Cited by 498
Chronic inflammation and the hallmarks of aging
Baechle, J. J., Chen, N., Makhijani, P., Winer, S., Furman, D., & Winer, D. A. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101755 · Cited by 471
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
Entezari, M., Hashemi, D., Taheriazam, A., Zabolian, A., Mohammadi, S., Fakhri, F., Hashemi, M., Hushmandi, K., Ashrafizadeh, M., Zarrabi, A., et al. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112563 · Cited by 410
RetractedAMP-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
Targeting AMPK for cancer prevention and treatment
Li, W., Saud, S. M., Young, M. R., Chen, G., & Hua, B. (2015) · Oncotarget · doi:10.18632/oncotarget.3629 · Cited by 361
The Crosstalk between the Gut Microbiota and Mitochondria during Exercise
Clark, A. P., & Mach, N. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00319 · Cited by 345
An AMPK–caspase-6 axis controls liver damage in nonalcoholic steatohepatitis
Zhao, P., Sun, X., Chaggan, C., Liao, Z., Wong, K. I., He, F., Singh, S., Loomba, R. S., Karin, M., Witztum, J. L., et al. (2020) · Science · doi:10.1126/science.aay0542 · Cited by 312
Mammalian/mechanistic target of rapamycin (mTOR) complexes in neurodegeneration
Querfurth, H., & Lee, H.-K. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00428-5 · Cited by 288
The AMPK Inhibitor Compound C Is a Potent AMPK-Independent Antiglioma Agent
Liu, X., Chhipa, R. R., Nakano, I., & Dasgupta, B. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0579 · Cited by 288
Lai, Y.-C., Tabima, D. M., Dube, J. J., Hughan, K. S., Vanderpool, R. R., Goncharov, D. A., St. Croix, C. M., Garcia-Ocaña, A., Goncharova, E. A., Tofovic, S. P., et al. (2016) · Circulation · doi:10.1161/circulationaha.115.018935 · Cited by 270
TBK1 at the Crossroads of Inflammation and Energy Homeostasis in Adipose Tissue
Zhao, P., Wong, K. I., Sun, X., Reilly, S. M., Uhm, M., Liao, Z., Skorobogatko, Y., & Saltiel, A. R. (2018) · Cell · doi:10.1016/j.cell.2018.01.007 · Cited by 250
AMP-activated protein kinase, stress responses and cardiovascular diseases
Wang, S., Song, P., & Zou, M. (2012) · Clinical Science · doi:10.1042/cs20110625 · Cited by 251
Uittenbogaard, M. N., & Chiaramello, A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305224906 · Cited by 246
AMPK improves gut epithelial differentiation and barrier function via regulating Cdx2 expression
Sun, X., Yang, Q., Rogers, C. J., Du, ., & Zhu, M. J. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.14 · Cited by 241
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
Self-citationSanli, T., Steinberg, G. R., Singh, G., & Tsakiridis, T. (2014) · Cancer Biology & Therapy · doi:10.4161/cbt.26726 · Cited by 220
Nandipati, K. C., Subramanian, S., & Agrawal, D. K. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2878-8 · Cited by 214
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.003 · Cited by 212
The relationship of autophagy defects to cartilage damage during joint aging in a mouse model
Caramés, B., Olmer, M., Kiosses, W. B., & Lotz, M. K. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39073 · Cited by 204
The role of AMPK in macrophage metabolism, function and polarisation
Cui, Y., Chen, J., Zhang, Z., Shi, H., Sun, W., & Yi, Q. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04772-6 · Cited by 213
Antonopoulos, A. S., Margaritis, M., Verheule, S., Récalde, A., Sanna, F., Herdman, L., Psarros, C. T., Nasrallah, H. M., Coutinho, P., Akoumianakis, I., et al. (2016) · Circulation Research · doi:10.1161/circresaha.115.307856 · Cited by 173
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
Negative regulation of AMPK signaling by high glucose via E3 ubiquitin ligase MG53
Jiang, P., Ren, L., Li, Z., Yu, Z., Lv, F., Xu, F., Peng, W., Bai, X., Cheng, K., Quan, L., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.008 · Cited by 170
SIRT3 Protects Against Acute Kidney Injury via AMPK/mTOR-Regulated Autophagy
Zhao, W., Zhang, L., Chen, R., Lu, H., Sui, M., Zhu, Y., & Zeng, L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01526 · Cited by 155
Jaganathan, R., Ravindran, R., & Dhanasekaran, S. (2017) · Canadian Journal of Diabetes · doi:10.1016/j.jcjd.2017.10.040 · Cited by 154
Long-chain fatty acyl-CoA esters regulate metabolism via allosteric control of AMPK β1 isoforms
Pinkosky, S. L., Scott, J. W., Desjardins, E. M., Smith, B. K., Day, E. A., Ford, R. J., Langendorf, C. G., Ling, N. X. Y., Nero, T. L., Loh, K., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0245-2 · Cited by 145
Prasad, S., Sajja, R. K., Kaisar, M. A., Park, J. H., Villalba, H., Liles, T., Abbruscato, T. J., & Cucullo, L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.007 · Cited by 138
A Metabolic Roadmap for Somatic Stem Cell Fate
Ly, C., Lynch, G. S., & Ryall, J. G. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.022 · Cited by 144
Critical Role for AMPK in Metabolic Disease-Induced Chronic Kidney Disease
Juszczak, F., Caron, N., Mathew, A. V., & Declèves, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217994 · Cited by 140
Role of AMPK activation in oxidative cell damage: Implications for alcohol-induced liver disease
Sid, B., Verrax, J., & Calderón, P. B. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.05.007 · Cited by 141
Lindholm, C. R., Ertel, R. L., Bauwens, J. D., Schmuck, E. G., Mulligan, J. D., & Saupe, K. W. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-012-0199-2 · Cited by 136
Hyporesponsiveness to the anti-inflammatory action of interleukin-10 in type 2 diabetes
Barry, J., Shakibakho, S., Durrer, C. G., Simtchouk, S., Jawanda, K. K., Cheung, S. T., Mui, A., & Little, J. P. (2016) · Scientific Reports · doi:10.1038/srep21244 · Cited by 136
Quercetin, a functional compound of onion peel, remodels white adipocytes to brown-like adipocytes
Lee, S. G., Parks, J. S., & Kang, H. W. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.12.018 · Cited by 130
ANGPTL4 mediates shuttling of lipid fuel to brown adipose tissue during sustained cold exposure
Dijk, W., Heine, M., Vergnes, L., Boon, M. R., Schaart, G., Hesselink, M. K., Reue, K., van Marken Lichtenbelt, W. D., Olivecrona, G., Rensen, P. C., et al. (2015) · eLife · doi:10.7554/elife.08428 · Cited by 114
AMP-activated protein kinase selectively inhibited by the type II inhibitor SBI-0206965
Dite, T. A., Langendorf, C. G., Hoque, A., Galić, S., Rebello, R. J., Ovens, A. J., Lindqvist, L., Ngoei, K. R. W., Ling, N. X. Y., Furic, L., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003547 · Cited by 132
On the Clinical Pharmacology of Reactive Oxygen Species
Casas, A. I., Nogales, C., Mucke, H. A., Petraina, A., Cuadrado, A., Rojo, A. I., Ghezzi, P., Jaquet, V., Augsburger, F., Dufrasne, F., et al. (2020) · Pharmacological Reviews · doi:10.1124/pr.120.019422 · Cited by 131
Zhang, M., Deng, Y., Zhang, J., Liu, J., Li, Y., Su, H., & Qu, Q. (2018) · Aging and Disease · doi:10.14336/ad.2017.0517 · Cited by 126
Zhuo, X., Wu, Y., Ni, Y.-J., Liu, J.-H., Gong, M., Wang, X.-H., Feng, W., Wang, T., Yuan, Z., Ma, A.-Q., et al. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0843-5 · Cited by 121
Evolving Lessons on the Complex Role of AMPK in Normal Physiology and Cancer
Dasgupta, B., & Chhipa, R. R. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.11.007 · Cited by 121
Gratia, S., Kay, L., Potenza, L., Seffouh, A., Novel-Chaté, V., Schnebelen, C., Sestili, P., Schlattner, U., & Tokarska-Schlattner, M. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs134 · Cited by 123
Lu, J., Shi, J., Li, M., Gui, B., Fu, R., Yao, G., Duan, Z., Lv, Z., Yang, Y., Chen, Z., et al. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.01.042 · Cited by 119
Moreira, D., Rodrigues, V., Abengózar, M. Á., Rivas, L., Rial, E., Laforge, M., Li, X., Foretz, M., Viollet, B., Estaquier, J., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004684 · Cited by 125
Self-citationTargeting ATP-Citrate Lyase in Hyperlipidemia and Metabolic Disorders
Pinkosky, S. L., Groot, P. H. E., Lalwani, N. D., & Steinberg, G. R. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.09.001 · Cited by 118
Regulation of NAD(P)H oxidases by AMPK in cardiovascular systems
Song, P., & Zou, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.025 · Cited by 122
Bigham, A. W., Julian, C. G., Wilson, M. J., Vargas, E., Browne, V. A., Shriver, M. D., & MOORE, L. G. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00063.2014 · Cited by 114
AMP-activated protein kinase: A target for old drugs against diabetes and cancer
Russo, G. L., Russo, M., & Ungaro, P. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.05.023 · Cited by 116
Chronic Activation of γ2 AMPK Induces Obesity and Reduces β Cell Function
Yavari, A., Stocker, C. J., Ghaffari, S., Wargent, E. T., Steeples, V., Czibik, G., Pintér, K., Bellahcene, M., Woods, A., de Morentin, P. B. M., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.003 · Cited by 114
Ma, Z., Dai, J., Zhang, W., Yuan, Y., Liao, H., Zhang, N., Bian, Z., & Tang, Q. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13449 · Cited by 109
Leishmania survival in the macrophage: where the ends justify the means
Duque, G. A., & Descoteaux, A. (2015) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.04.007 · Cited by 116
Lee, J. H., Kim, J. H., Kim, J. S., Chang, J. W., Kim, S. B., Park, J. S., & Lee, S. K. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00148.2012 · Cited by 107
mTOR, AMPK, and Sirt1: Key Players in Metabolic Stress Management
Cetrullo, S., D’Adamo, S., Tantini, B., Borzı̀, R. M., & Flamigni, F. (2015) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2015012975 · Cited by 109
Mancini, S. J., White, A. D., Bijland, S., Rutherford, C. L., Graham, D., Richter, E. A., Viollet, B., Touyz, R. M., Palmer, T. M., & Salt, I. P. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.11.010 · Cited by 106
Self-citationZois, C. E., Favaro, E., & Harris, A. L. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.09.001 · Cited by 102
Gui, D., Cui, Z., Zhang, L., Chang, Y., Yao, D., Xu, M., Chen, M., Wu, P., Li, G., Wang, L., et al. (2017) · BMC Pulmonary Medicine · doi:10.1186/s12890-017-0477-4 · Cited by 100
Chen, R. R., Yung, M. M. H., Yang, X., Zhan, S., Leung, L. L., Liang, R. R., Leung, T. H. Y., Yang, H., Xu, D., Sharma, R., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0508-1 · Cited by 97
Zhao, P., & Saltiel, A. R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011356 · Cited by 106
Noise-Induced Loss of Hair Cells and Cochlear Synaptopathy Are Mediated by the Activation of AMPK
Hill, K., Yuan, H., Wang, X., & Sha, S. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0782-16.2016 · Cited by 97
Ye, D., Zhang, M., Zhang, W., Lu, Q., Cai, Z., Song, P., Okon, I. S., Xiao, L., & Zou, M. (2016) · Circulation Research · doi:10.1161/circresaha.116.308689 · Cited by 96
Zha, Q.-B., Wei, H.-X., Li, C.-G., Liang, Y.-D., Xu, L.-H., Bai, W.-J., Pan, H., He, X.-H., & Ouyang, D.-Y. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00597 · Cited by 95
AMPKα2 Deletion Exacerbates Neointima Formation by Upregulating Skp2 in Vascular Smooth Muscle Cells
Song, P., Wang, S., He, C., Wang, S., Liang, B., Viollet, B., & Zou, M. (2011) · Circulation Research · doi:10.1161/circresaha.111.250423 · Cited by 92
Self-citationRetractedAsby, D. J., Cuda, F., Beyaert, M., Houghton, F. D., Cagampang, F. R. A., & Tavassoli, A. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.06.008 · Cited by 91
Xu, C., Liu, W., Zhang, D., Cao, X., Shi, H., & Li, X. (2017) · Aquaculture · doi:10.1016/j.aquaculture.2017.10.022 · Cited by 91
Tang, T., Song, J., Li, J., Wang, H., Zhang, Y., & Suo, H. (2020) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2020.116398 · Cited by 89
Satriano, J. A., Sharma, K., Blantz, R. C., & Deng, A. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00293.2013 · Cited by 87
He, M. X., Zhang, Q., Deng, C., Wang, H., Lian, J., & Huang, X. (2014) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2014.01.018 · Cited by 93
Brain-specific repression of AMPKα1 alleviates pathophysiology in Alzheimer’s model mice
Zimmermann, H. R., Yang, W., Kasica, N. P., Zhou, X., Wang, X., Beckelman, B. C., Lee, J., Furdui, C. M., Keene, C. D., & Ma, T. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133982 · Cited by 86
The immunomodulatory role of irisin on osteogenesis via AMPK-mediated macrophage polarization
Ye, W., Wang, J., Lin, D., & Ding, Z. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.12.028 · Cited by 86
Liu, C., Guo, Y., Sun, L., Lai, X., Li, Q., Zhang, W., Xiang, L., Sun, S., & Cao, F. (2019) · Food & Function · doi:10.1039/c8fo02334d · Cited by 86
AMP-Activated Protein Kinase and Host Defense against Infection
Silwal, P., Kim, J. K., Yuk, J., & Jo, E. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113495 · Cited by 82
Quercetin induces bladder cancer cells apoptosis by activation of AMPK signaling pathway.
Su, Q., Peng, M., Zhang, Y., Xu, W., Darko, K. O., Tao, T., Huang, Y., Tao, X., & Yang, X. (2016) · PubMed Central · Cited by 83
Vingtdeux, V., Chandakkar, P., Zhao, H., Davies, P., & Marambaud, P. (2011) · Molecular Medicine · doi:10.2119/molmed.2011.00163 · Cited by 81
Atrial remodelling in atrial fibrillation: CaMKII as a nodal proarrhythmic signal
Mesubi, O. O., & Anderson, M. E. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw002 · Cited by 81
Cusi, K. J., Alkhouri, N., Harrison, S. A., Fouqueray, P., Moller, D. E., Hallakou‐Bozec, S., Bolze, S., Grouin, J., Megnien, S. J., Dubourg, J., et al. (2021) · The Lancet. Gastroenterology & hepatology · doi:10.1016/s2468-1253(21)00300-9 · Cited by 80
Metformin-stimulated AMPK-α1 promotes microvascular repair in acute lung injury
Jian, M., ALEXEYEV, M. F., Wolkowicz, P. E., Zmijewski, J. W., & Creighton, J. R. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00173.2013 · Cited by 78
Gautam, J., Khedgikar, V., Kushwaha, P., Choudhary, D., Nagar, G. K., Dev, K., Dixit, P., Singh, D. R., Maurya, R., & Trivedi, R. (2017) · British Journal Of Nutrition · doi:10.1017/s0007114517000149 · Cited by 78
Tosca, L., Froment, P., Ramé, C., McNEILLY, J. R., McNeilly, A. S., Maillard, V., & Dupont, J. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.110.087023 · Cited by 83
Arrhythmia causes lipid accumulation and reduced glucose uptake
Lenski, M., Schleider, G., Kohlhaas, M., Adrian, L., Adam, O., Tian, X. Y., Kaestner, L., Lipp, P., Lehrke, M., Maack, C., et al. (2015) · Basic Research in Cardiology · doi:10.1007/s00395-015-0497-2 · Cited by 76
Johnson, R., de Beer, D., Dludla, P. V., Ferreira, D., Muller, C. J. F., & Joubert, E. (2018) · Planta Medica · doi:10.1055/s-0044-100622 · Cited by 79
The Bewildering Effect of AMPK Activators in Alzheimer’s Disease: Review of the Current Evidence
Assefa, B. T., Tafere, G. G., Wondafrash, D. Z., & Gidey, M. T. (2020) · BioMed Research International · doi:10.1155/2020/9895121 · Cited by 76
AMP-activated protein kinase: Structure, function, and role in pathological processes
Novikova, D., Garabadzhiu, A. V., Melino, G., Barlev, N. A., & Tribulovich, V. G. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915020017 · Cited by 77
Kwon, B., & Querfurth, H. W. (2015) · Biochimie · doi:10.1016/j.biochi.2015.09.006 · Cited by 77
A spatiotemporal hypothesis for the regulation, role, and targeting of AMPK in prostate cancer
Khan, A., & Frigo, D. E. (2017) · Nature Reviews Urology · doi:10.1038/nrurol.2016.272 · Cited by 74
Lee, M.-S., Han, H.-J., Han, S. Y., Kim, I. Y., Chae, S., Lee, C.-S., Kim, S. E., Yoon, S. G., Park, J.-W., Kim, J.-H., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05721-4 · Cited by 75
An, H., Jang, Y., Choi, J.-I., Hur, J., Kim, S., & Kwon, Y. (2024) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2024.188 · Cited by 75
Hypoxia, AMPK activation and uterine artery vasoreactivity
Skeffington, K. L., Higgins, J. S., Mahmoud, A. D., Evans, A. M., Sferruzzi‐Perri, A. N., Fowden, A. L., Yung, H. W., Burton, G. J., Giussani, D. A., & Moore, L. G. (2016) · The Journal of Physiology · doi:10.1113/jp270995 · Cited by 69
Laderoute, K. R., Calaoagan, J. M., Chao, W., Dinh, D., Denko, N. C., Duellman, S. J., Kalra, J., Liu, X., Papandreou, I., Sambucetti, L. C., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576371 · Cited by 69
Nuclear Transport: A Switch for the Oxidative Stress—Signaling Circuit?
Kodiha, M., & Stochaj, U. (2011) · Journal of Signal Transduction · doi:10.1155/2012/208650 · Cited by 72
von Loeffelholz, C., Coldewey, S. M., & Birkenfeld, A. L. (2021) · Cells · doi:10.3390/cells10071822 · Cited by 70
Metformin activation of AMPK suppresses AGE-induced inflammatory response in hNSCs
Chung, M.-M., Nicol, C. J., Cheng, Y.-C., Lin, K.-H., Chen, Y.-L., Pei, D., Lin, C.-H., Shih, Y.-N., Yen, C.-H., Chen, S.-J., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.01.017 · Cited by 66
Kim, S. Y., Jeong, S., Jung, E., Baik, K.-H., Chang, M. H., Kim, S. A., Shim, J.-H., Chun, E., & Lee, K. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.95 · Cited by 66
AMP-activated protein kinase: a therapeutic target in intestinal diseases
Sun, X., & Zhu, M. J. (2017) · Open Biology · doi:10.1098/rsob.170104 · Cited by 68
Saha, M., Kumar, S., Bukhari, S., Andugulapati, S. B., Kumar, P., Hindupur, S. K., & Rangarajan, A. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2090 · Cited by 66
Mangalam, A. K. (2013) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000150 · Cited by 65
Have guidelines addressing physical activity been established in nonalcoholic fatty liver disease?
Finelli, C. (2012) · World Journal of Gastroenterology · doi:10.3748/wjg.v18.i46.6790 · Cited by 63
Scott, J. W., Galić, S., Graham, K. L., Foitzik, R. C., Ling, N. X. Y., Dite, T. A., Issa, S. M. A., Langendorf, C. G., Weng, Q. P., Thomas, H. E., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.011 · Cited by 61
AMPK Inhibition Blocks ROS-NFκB Signaling and Attenuates Endotoxemia-Induced Liver Injury
Guo, Y., Zhang, Y., Hong, K. M., Luo, F., Gu, Q., Lü, N., & Bai, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086881 · Cited by 61
Metadata
- Authors
- Viollet, B., Horman, S., Leclerc, J., Lantier, L., Foretz, M., Billaud, M., Giri, S., & Andreelli, F.
- Affiliations
- UCLouvain (BE)
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Mayo Clinic (US)
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 2010-06-04
- Volume
- 45
- Issue
- 4
- Pages
- 276-295
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- PMC
- PMC3132561
- OpenAlex
- W2015171350
- Cited by
- 383
- References
- 226
- Citations by year
- 2026: 14 · 2025: 15 · 2024: 11 · 2023: 18 · 2022: 22 · 2021: 23 · 2020: 39 · 2019: 22 · 2018: 34 · 2017: 33 · 2016: 38 · 2015: 30 · 2014: 27 · 2013: 25 · 2012: 19
- FWCI
- 1.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Critical Reviews in Biochemistry and Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion, other-oa)
- Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion, other-oa)
- Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion)
- Funders
- European Commission
- Agence Nationale de la Recherche (ANR-06-PHYS-0026)
- 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 › Peroxisome Proliferator-Activated Receptors
- Keywords
- AMPK, AMPK inhibition, energy homeostasis, allosteric regulation, protein phosphorylation, central nervous system metabolism
- MeSH terms
- Animals, Energy Metabolism, Enzyme Activation, Humans, Down-Regulation, AMP-Activated Protein Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review