The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
AMPK β1 Deletion Reduces Appetite, Preventing Obesity and Hepatic Insulin Resistance
Open accessAbstract
The AMP-activated protein kinase (AMPK) is an alphabetagamma heterotrimer that regulates appetite and fuel metabolism. We have generated AMPK beta1(-/-) mice on a C57Bl/6 background that are viable, fertile, survived greater than 2 years, and display no visible brain developmental defects. These mice have a 90% reduction in hepatic AMPK activity due to loss of the catalytic alpha subunits, with modest reductions of activity detected in the hypothalamus and white adipose tissue and no change in skeletal muscle or heart. On a low fat or an obesity-inducing high fat diet, beta1(-/-) mice had reduced food intake, reduced adiposity, and reduced total body mass. Metabolic rate, physical activity, adipose tissue lipolysis, and lipogenesis were similar to wild type littermates. The reduced appetite and body mass of beta1(-/-) mice were associated with protection from high fat diet-induced hyperinsulinemia, hepatic steatosis, and insulin resistance. We demonstrate that the loss of beta1 reduces food intake and protects against the deleterious effects of an obesity-inducing diet.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“AMPK β1 KO mice have reduced AMPK activity in liver but not skeletal muscle, are hyperphagic and as a result have lower body weight, adiposity and hepatic lipid accumulation, and are protected from high-fat diet induced insulin resistance [27].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [27]
In the citing paper
“AMPK β1 KO mice have reduced AMPK activity in liver but not skeletal muscle, are hyperphagic and as a result have lower body weight, adiposity and hepatic lipid accumulation, and are protected from high-fat diet induced insulin resistance [27].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [27]
Citations
Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
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
Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB
Cai, D., Yuan, M., Frantz, D. F., Melendez, P. A., Hansen, L., Lee, J., & Shoelson, S. E. (2005) · Nature Medicine · doi:10.1038/nm1166 · Cited by 2,245
The 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
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
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., 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
The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
Koo, S., Flechner, L., Qi, L., Zhang, X., Screaton, R. A., Jeffries, S., Hedrick, S. A., Xu, W., Boussouar, F., Brindle, P. K., et al. (2005) · Nature · doi:10.1038/nature03967 · Cited by 1,026
Petersen, K. F., Dufour, S., Befroy, D., Lehrke, M., Hendler, R. E., & Shulman, G. I. (2005) · Diabetes · doi:10.2337/diabetes.54.3.603 · Cited by 911
AMP-activated Protein Kinase Plays a Role in the Control of Food Intake
Andersson-Hall, U. K., Filipsson, K., Abbott, C. R., Woods, A., Smith, K. L., Bloom, S. R., Carling, D., & Small, C. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300557200 · Cited by 777
Flagged first, then by citations
Research works printed but not linked: 1
- Altschul, 1990, J. Mol. Biol., 215, 403, 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
Cited by
Sorted by citations
New insights into activation and function of the AMPK
Steinberg, G. R., & Hardie, D. G. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00547-x · Cited by 1,047
Self-citationFullerton, M. D., Galic, S., Marcinko, K., Sikkema, S., Pulinilkunnil, T., Chen, Z.-P., O'Neill, H. M., Ford, R. J., Palanivel, R., O'Brien, M., et al. (2013) · Nature Medicine · doi:10.1038/nm.3372 · Cited by 893
Self-citationAMP-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
Self-citationThe 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
Self-citationHypothalamic AMPK and fatty acid metabolism mediate thyroid regulation of energy balance
López, M., Varela, L., Vazquez, M. J., Rodríguez‐Cuenca, S., González, C. R., Velagapudi, V., Morgan, D. A., Schoenmakers, E., Agassandian, K., Lage, R., et al. (2010) · Nature Medicine · doi:10.1038/nm.2207 · Cited by 686
AMPK as a Therapeutic Target for Treating Metabolic Diseases
Day, E. A., Ford, R. J., & Steinberg, G. R. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.05.004 · Cited by 630
Self-citationPI3K/AKT, MAPK and AMPK signalling: protein kinases in glucose homeostasis
Schultze, S. M., Hemmings, B. A., Nießen, M., & Tschopp, O. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002109 · Cited by 553
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
Self-citationO'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
Self-citationGalić, S., Fullerton, M. D., Schertzer, J. D., Sikkema, S. R., Marcinko, K., Walkley, C. R., Izon, D. J., Honeyman, J. E., Chen, Z., van Denderen, B. J., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci58577 · Cited by 352
Self-citationMottillo, E. P., Desjardins, E. M., Crane, J. D., Smith, B. K., Green, A. E., Ducommun, S., Henriksen, T. I., Rebalka, I. A., Razi, A., Sakamoto, K., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.006 · Cited by 338
Self-citationHypothalamic AMPK: a canonical regulator of whole-body energy balance
López, M., Nogueiras, R., Tena‐Sempere, M., & Diéguez, C. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.67 · Cited by 318
Day, E. A., Ford, R. J., Smith, B. K., Mohammadi-Shemirani, P., Morrow, M. R., Gutgesell, R. M., Lu, R., Raphenya, A. R., Kabiri, M., McArthur, A. G., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0146-4 · Cited by 307
Self-citationAMPK and Exercise: Glucose Uptake and Insulin Sensitivity
O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295
Role of AMP-activated protein kinase in adipose tissue metabolism and inflammation
Bijland, S., Mancini, S. J., & Salt, I. P. (2013) · Clinical Science · doi:10.1042/cs20120536 · Cited by 293
Leptin's Role in Lipodystrophic and Nonlipodystrophic Insulin-Resistant and Diabetic Individuals
Moon, H., Dalamaga, Μ., Kim, S. Y., Pοlyzos, S. A., Hamnvik, O. R., Magkos, F., Paruthi, J., & Mantzoros, C. S. (2013) · Endocrine Reviews · doi:10.1210/er.2012-1053 · Cited by 265
NOD1 activators link innate immunity to insulin resistance
Schertzer, J. D., Tamrakar, A. K., Magalhães, J. G., Pereira, S., Bilan, P. J., Fullerton, M. D., Liu, Z., Steinberg, G. R., Giacca, A., Philpott, D. J., et al. (2011) · Diabetes · doi:10.2337/db11-0004 · Cited by 253
Self-citationVillani, L. A., Smith, B. K., Marcinko, K., Ford, R. J., Broadfield, L. A., Green, A. E., Houde, V. P., Muti, P. C., Tsakiridis, T. K., & Steinberg, G. R. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.08.014 · Cited by 247
Self-citationMeakin, P. J., Chowdhry, S., Sharma, R. S., Ashford, F. B., Walsh, S. V., McCrimmon, R. J., Dinkova‐Kostova, A. T., Dillon, J. F., Hayes, J. D., & Ashford, M. L. J. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00677-14 · Cited by 233
Inhibition of Hypothalamic Inflammation Reverses Diet-Induced Insulin Resistance in the Liver
Milanski, M., Arruda, A. P., Coope, A., Ignácio-Souza, L. M., Nuñez, C. E. C., Roman, E. A., Romanatto, T., Pascoal, L. B., Caricilli, A. M., Torsoni, M. A., et al. (2012) · Diabetes · doi:10.2337/db11-0390 · Cited by 233
Sanli, T., Steinberg, G. R., Singh, G., & Tsakiridis, T. (2014) · Cancer Biology & Therapy · doi:10.4161/cbt.26726 · Cited by 220
Self-citationAdipose tissue: between the extremes
Vegiopoulos, A., Rohm, M., & Herzig, S. (2017) · The EMBO Journal · doi:10.15252/embj.201696206 · Cited by 214
Chan, K. L., Pillon, N. J., Sivaloganathan, D. M., Costford, S. R., Liu, Z., Théret, M., Chazaud, B., & Klip, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.646992 · Cited by 196
Lu, J. L., Wu, D., Zheng, Y., Hu, B., Zhang, Z., Shan, Q., Zheng, Z., Liu, C., & Wang, Y. (2010) · The Journal of Pathology · doi:10.1002/path.2754 · Cited by 186
mTOR signaling in tumorigenesis
Xu, K. L., Liu, P., & Wei, W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.10.007 · Cited by 167
Steinberg, G. R., O'Neill, H. M., Dzamko, N. L., Galic, S., Naim, T., Koopman, R., Jørgensen, S. B., Honeyman, J., Hewitt, K., Chen, Z.-P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102434 · Cited by 164
Self-citationFord, R. J., Fullerton, M. D., Pinkosky, S. L., Day, E. A., Scott, J. W., Oakhill, J. S., Bujak, A. L., Smith, B. K., Crane, J. D., Blümer, R. M. E., et al. (2015) · Biochemical Journal · doi:10.1042/bj20150125 · Cited by 164
Self-citationRohm, M., Schäfer, M., Laurent, V., Üstünel, B. E., Niopek, K., Algire, C., Hautzinger, O., Sijmonsma, T., Zota, A., Medříková, D., et al. (2016) · Nature Medicine · doi:10.1038/nm.4171 · Cited by 153
Self-citationDeletion of Skeletal Muscle SOCS3 Prevents Insulin Resistance in Obesity
Jørgensen, S. B., O’Neill, H. M., Sylow, L., Honeyman, J. E., Hewitt, K. A., Palanivel, R., Fullerton, M. D., Öberg, L., Balendran, A., Galić, S., et al. (2012) · Diabetes · doi:10.2337/db12-0443 · Cited by 152
Self-citationEsquejo, R. M., Salatto, C. T., Delmore, J. E., Albuquerque, B., Reyes, A. R., Shi, Y., Moccia, R., Cokorinos, E., Peloquin, M., Monetti, M., et al. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.04.009 · Cited by 152
Self-citationWan, Z., Root-McCaig, J., Castellani, L. N., Kemp, B. E., Steinberg, G. R., & Wright, D. C. (2013) · Obesity · doi:10.1002/oby.20605 · Cited by 150
Self-citationLong-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
Self-citationWilliams, T., Courchet, J., Viollet, B., Brenman, J. E., & Polleux, F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013660108 · Cited by 123
Mechanism of Action of Compound-13: An α1-Selective Small Molecule Activator of AMPK
Hunter, R. W., Foretz, M., Bultot, L., Fullerton, M. D., Deák, M., Ross, F. A., Hawley, S. A., Shpiro, N., Viollet, B., Barron, D., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.05.014 · Cited by 132
Self-citationEvolving 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
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
Lebeau, P. F., Byun, J. H., Platko, K., Saliba, P., Sguazzin, M. A., MacDonald, M. E., Paré, G., Steinberg, G. R., Janssen, L. J., Igdoura, S. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28240-9 · Cited by 113
Self-citationRole of SIRT1 and AMPK in mesenchymal stem cells differentiation
Chen, H., Liu, X., Chen, H., Cao, J., Zhang, L., Hu, X., & Wang, J. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.12.002 · Cited by 109
The role of AMP-activated protein kinase in regulating white adipose tissue metabolism
Ceddia, R. B. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.014 · Cited by 105
Altered Metabolism and Persistent Starvation Behaviors Caused by Reduced AMPK Function in Drosophila
Johnson, E. C., Kazgan, N., Bretz, C. A., Forsberg, L. J., Hector, C. E., Worthen, R. J., Onyenwoke, R. U., & Brenman, J. E. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012799 · Cited by 105
Ding, X., Jian, T., Li, J., Lv, H., Tong, B., Li, J., Meng, X., Ren, B., & Chen, J. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/9734560 · Cited by 103
Sachithanandan, N., Fam, B. C., Fynch, S., Dzamko, N. L., Watt, M. J., Wormald, S., Honeyman, J. E., Galić, S., Proietto, J., Andrikopoulos, S., et al. (2010) · Hepatology · doi:10.1002/hep.23861 · Cited by 107
Self-citationAMPK and the Endocrine Control of Metabolism
Townsend, L. K., & Steinberg, G. R. (2023) · Endocrine Reviews · doi:10.1210/endrev/bnad012 · Cited by 114
Self-citationEmerging role of AMP-activated protein kinase in endocrine control of metabolism in the liver
Hasenour, C. M., Berglund, E. D., & Wasserman, D. H. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.018 · Cited by 100
El-Assaad, W., Joly, E. C., Barbeau, A., SLADEK, R. M., Buteau, J., Maestre, I., Pépin, É., Zhao, S., Iglesias, J., Roche, E., et al. (2010) · Endocrinology · doi:10.1210/en.2009-1238 · Cited by 96
The role of ampk in controlling metabolism and mitochondrial biogenesis during exercise
Marcinko, K., & Steinberg, G. R. (2014) · Experimental Physiology · doi:10.1113/expphysiol.2014.082255 · Cited by 92
Self-citationHypothalamic 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
ATP-citrate lyase: genetics, molecular biology and therapeutic target for dyslipidemia
Burke, A. C., & Huff, M. W. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000390 · Cited by 91
O’Brien, A. J., Villani, L. A., Broadfield, L. A., Houde, V. P., Galić, S., Blandino, G., Kemp, B. E., Tsakiridis, T. K., Muti, P. C., & Steinberg, G. R. (2015) · Biochemical Journal · doi:10.1042/bj20150122 · Cited by 90
Self-citationLoh, K., Tam, S., Murray‐Segal, L., Huynh, K., Meikle, P. J., Scott, J. W., van Denderen, B., Chen, Z., Steel, R., LeBlond, N. D., et al. (2018) · Hepatology Communications · doi:10.1002/hep4.1279 · Cited by 89
Self-citationChrysostomou, V., Galić, S., van Wijngaarden, P., Trounce, I. A., Steinberg, G. R., & Crowston, J. G. (2016) · Aging Cell · doi:10.1111/acel.12512 · Cited by 89
Self-citationHypothalamic AMP-Activated Protein Kinase Regulates Glucose Production
Yang, C. S., Lam, C. K. L., Chari, M., Cheung, G. W. C., Kokorovic, A., Gao, S., Leclerc, I., Rutter, G. A., & Lam, T. K. T. (2010) · Diabetes · doi:10.2337/db10-0221 · Cited by 86
CAMKK2 Promotes Prostate Cancer Independently of AMPK via Increased Lipogenesis
Penfold, L., Woods, A., Muckett, P. J., Nikitin, A. Y., Kent, T. R., Zhang, S., Graham, R., Pollard, A., & Carling, D. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0585 · Cited by 81
Sachithanandan, N., Graham, K. L., Galic, S., Honeyman, J. E., Fynch, S. L., Hewitt, K. A., Steinberg, G. R., & Kay, T. W. (2011) · Diabetes · doi:10.2337/db11-0259 · Cited by 81
Self-citationEnhanced activation of cellular AMPK by dual-small molecule treatment: AICAR and A769662
Ducommun, S., Ford, R. J., Bultot, L., Deák, M., Bertrand, L., Kemp, B. E., Steinberg, G. R., & Sakamoto, K. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00672.2013 · Cited by 83
Self-citationA big-data approach to understanding metabolic rate and response to obesity in laboratory mice
Corrigan, J. K., Ramachandran, D., He, Y., Palmer, C. J., Jurczak, M. J., Chen, R., Li, B., Friedline, R. H., Kim, J. K., Ramsey, J. J., et al. (2020) · eLife · doi:10.7554/elife.53560 · Cited by 86
Kim, H., Park, J., Jung, Y., Ahn, K. S., & Um, J. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.09.227 · Cited by 80
Krishan, S., Richardson, D. R., & Sahni, S. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.095810 · Cited by 80
Saito, M., Saito, M., & Das, B. C. (2019) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2019.01.007 · Cited by 75
Briggs, D. I., Lockie, S., Benzler, J., Wu, Q., Stark, R., Reichenbach, A., Hoy, A., Lemus, M., Coleman, H., Parkington, H., et al. (2014) · Endocrinology · doi:10.1210/en.2013-1861 · Cited by 72
Creatine maintains intestinal homeostasis and protects against colitis
Turer, E. E., McAlpine, W., Wang, K.-W., Lu, T., Li, X., Tang, M., Zhan, X., Wang, T., Zhan, X., Bu, C.-H., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1621400114 · Cited by 76
Bojic, L. A., Telford, D. E., Fullerton, M. D., Ford, R. J., Sutherland, B. G., Edwards, J. Y., Sawyez, C. G., Gros, R., Kemp, B. E., Steinberg, G. R., et al. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m046037 · Cited by 74
Self-citationFunction of the master energy regulator adenosine monophosphate‐activated protein kinase in stroke
Manwani, B., & McCullough, L. D. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23207 · Cited by 76
Bultot, L., Jensen, T. E., Lai, Y., Madsen, A. B., Collodet, C., Kviklyte, S., Deák, M., Yavari, A., Foretz, M., Ghaffari, S., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00237.2016 · Cited by 82
Morrow, N. M., Burke, A. C., Samsoondar, J. P., Seigel, K. E., Wang, A., Telford, D. E., Sutherland, B. G., O’Dwyer, C., Steinberg, G. R., Fullerton, M. D., et al. (2020) · Journal of Lipid Research · doi:10.1194/jlr.ra119000542 · Cited by 70
Self-citationSalicylate 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
Self-citationvon Loeffelholz, C., Coldewey, S. M., & Birkenfeld, A. L. (2021) · Cells · doi:10.3390/cells10071822 · Cited by 70
Li, N., Yin, L., Shang, J., Liang, M., Liu, Z., Yang, H., Qiang, G., Du, G., & Yang, X. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115113 · Cited by 71
Bempedoic acid: effects on lipoprotein metabolism and atherosclerosis
Burke, A. C., Telford, D. E., & Huff, M. W. (2018) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000565 · Cited by 67
The metabolic sensor AMPK: Twelve enzymes in one
Smiles, W. J., Ovens, A. J., Oakhill, J. S., & Kofler, B. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.102042 · Cited by 69
AMPK activation regulates neuronal structure in developing hippocampal neurons
Ramamurthy, S., Chang, E., Cao, Y., Zhu, J., & Ronnett, G. V. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2013.11.048 · Cited by 65
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
Self-citationAMPK-dependent modulation of hepatic lipid metabolism by nesfatin-1
Yin, Y., Li, Z., Gao, L., Li, Y., Zhao, J., & Zhang, W. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.09.006 · Cited by 62
AMP-Activated Protein Kinase (AMPK) and Energy-Sensing in the Brain
Ramamurthy, S., & Ronnett, G. V. (2012) · Experimental Neurobiology · doi:10.5607/en.2012.21.2.52 · Cited by 62
Hughey, C. C., James, F. D., Bracy, D. P., Donahue, E. P., Young, J. D., Viollet, B., Foretz, M., & Wasserman, D. H. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.811547 · Cited by 56
Yu, L., Gong, L., Wang, C., Hu, N., Tang, Y.-Q., Li, Z., Dai, X., & Li, Y. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s243893 · Cited by 57
Zhang, X., Wang, Z., Li, J., Gu, D., Li, S., Shen, C., & Song, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070663 · Cited by 58
Salicylates Ameliorate Intestinal Inflammation by Activating Macrophage AMPK.
Banskota, S., Wang, H.-Q., Kwon, Y. H., Gautam, J., Gurung, P., Haq, S., Hassan, F. M. N., Bowdish, D., Kim, J.-A., Carling, D., et al. (2020) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izaa305 · Cited by 41
Self-citationAMPK beta subunits: more than just a scaffold in the formation of AMPK complex
Sanz, P., Rubio, T., & García-Gimeno, M. A. (2013) · FEBS Journal · doi:10.1111/febs.12364 · Cited by 57
Homocysteine suppresses lipolysis in adipocytes by activating the AMPK pathway
Wang, Z., Pini, M., Yao, T., Zhou, Z., Sun, C., Fantuzzi, G., & Song, Z. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00050.2011 · Cited by 52
Palanivel, R., Fullerton, M. D., Galić, S., Honeyman, J. E., Hewitt, K., Jørgensen, S. B., & Steinberg, G. R. (2012) · Diabetologia · doi:10.1007/s00125-012-2665-3 · Cited by 53
Self-citationRao, Y., Liu, H., Gao, L., Yu, H., Tan, J., Ou, T., Huang, S., Gu, L., Ye, J., & Huang, Z. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.05.057 · Cited by 50
AMPK mediates energetic stress‐induced liver GDF15
Townsend, L. K., Weber, A. J., Day, E. A., Shamshoum, H., Shaw, S. J., Perry, C. G. R., Kemp, B. E., Steinberg, G. R., & Wright, D. C. (2020) · The FASEB Journal · doi:10.1096/fj.202000954r · Cited by 48
Self-citationLiou, T., Chen, H., Wang, W., Wu, S., Lee, Y.-C., Yang, W., & Lee, W. (2011) · Obesity Surgery · doi:10.1007/s11695-011-0457-3 · Cited by 45
Desjardins, E. M., Smith, B. K., Day, E. A., Ducommun, S., Sanders, M. J., Nederveen, J. P., Ford, R. J., Pinkosky, S. L., Townsend, L. K., Gutgesell, R. M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2119824119 · Cited by 47
Self-citationAMPK regulates macrophage polarization in adipose tissue inflammation and NASH
Weng, S., & Schuppan, D. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.09.031 · Cited by 45
AMPK β1 reduces tumor progression and improves survival in p53 null mice
Houde, V. P., Donzelli, S., Sacconi, A., Galić, S., Hammill, J. A., Bramson, J. L., Foster, R. A., Tsakiridis, T. K., Kemp, B. E., Grasso, G., et al. (2017) · Molecular Oncology · doi:10.1002/1878-0261.12079 · Cited by 41
Self-citationThe Outcome of Renal Ischemia-Reperfusion Injury Is Unchanged in AMPK-β1 Deficient Mice
Mount, P. F., Gleich, K., Tam, S., Fraser, S. A., Choy, S., Dwyer, K. M., Lü, B., van Denderen, B., Fingerle‐Rowson, G., Bucala, R., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029887 · Cited by 41
Self-citationBasseri, S., Lhoták, Š., Fullerton, M. D., Palanivel, R., Jiang, H. L., Lynn, E. G., Ford, R. J., Maclean, K. N., Steinberg, G. R., & Austin, R. C. (2012) · Diabetes · doi:10.2337/db12-0256 · Cited by 40
Self-citationDay, E. A., Ford, R. J., Lu, J. H., Lu, R., Lundenberg, L., Desjardins, E. M., Green, A. E., Lally, J., Schertzer, J. D., & Steinberg, G. R. (2020) · Biochemical Journal · doi:10.1042/bcj20200278 · Cited by 41
Self-citationXu, H., Liu, M., Liu, H., Zhao, B., Zheng, M., & Liu, J. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104582 · Cited by 43
Lee, M. K. S., Cooney, O. D., Lin, X., Nadarajah, S., Dragoljevic, D., Huynh, K., Onda, D.-A., Galić, S., Meikle, P. J., Edlund, H., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101514 · Cited by 38
Self-citationAMPK inhibits liver gluconeogenesis: fact or fiction?
Johanns, M., Hue, L., & Rider, M. H. (2023) · Biochemical Journal · doi:10.1042/bcj20220582 · Cited by 46
Christensen, M. S., Jensen, J., Jakobsen, S., Jessen, N., Frøkiær, J., Kemp, B. E., Marciszyn, A. L., Li, H., Pastor‐Soler, N. M., Hallows, K. R., et al. (2016) · Scientific Reports · doi:10.1038/srep35952 · Cited by 37
Self-citationKwon, M., Lim, S.-J., Joung, E., Lee, B., Oh, C., & Kim, H. (2018) · Journal of Functional Foods · doi:10.1016/j.jff.2018.05.063 · Cited by 37
CB1 receptor mediates the effects of glucocorticoids on AMPK activity in the hypothalamus
Scerif, M., Füzesi, T., Thomas, J., Kola, B., Grossman, A. B., Fekete, C., & Korbonits, M. (2013) · Journal of Endocrinology · doi:10.1530/joe-13-0192 · Cited by 36
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
Liu, L., & LiXian, Z. (2012) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.2012.12153 · Cited by 33
Targeting AMPK Signaling in the Liver: Implications for Obesity and Type 2 Diabetes Mellitus
Liu, Y., Wang, D., & Yang, L. (2022) · Current Drug Targets · doi:10.2174/1389450123666220429082702 · Cited by 35
Versatile Roles of LKB1 Kinase Signaling in Neural Development and Homeostasis
Kuwako, K.-I., & Okano, H. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00354 · Cited by 29
Metadata
- Authors
- Dzamko, N., van Denderen, B. J. W., Hevener, A. L., Jørgensen, S. B., Honeyman, J., Galic, S., Chen, Z.-P., Watt, M. J., Campbell, D. J., Steinberg, G. R., & Kemp, B. E.
- Affiliations
- The University of Melbourne (AU)
- University of California, Los Angeles (US)
- University of Copenhagen (DK)
- Monash University (AU)
- Corresponding author
- Steinberg, Gregory R.
- Kemp, Bruce E.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 285
- Issue
- 1
- Pages
- 115-122
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2804155
- OpenAlex
- W2028308875
- Cited by
- 175
- References
- 43
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 7 · 2022: 12 · 2021: 11 · 2020: 13 · 2019: 8 · 2018: 10 · 2017: 9 · 2016: 16 · 2015: 9 · 2014: 14 · 2013: 15 · 2012: 15
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Regulation of Appetite and Obesity
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- AMPK, appetite regulation, dietary intake, obesity, hepatic insulin resistance, hyperinsulinemia, hepatic steatosis, high-fat diet, knockout mice, adipose tissue lipolysis, lipogenesis, metabolic rate
- MeSH terms
- AMP-Activated Protein Kinase Kinases, Animals, Appetite, Body Weight, Carbon Dioxide, Darkness, Dietary Fats, Fasting, Feeding Behavior, Gene Expression Regulation, Gluconeogenesis, Insulin, Insulin Resistance, Liver, Mice, Inbred C57BL, Obesity, Organ Specificity, Oxidation-Reduction, Oxygen, Protein Kinases, Respiration, Gene Deletion, Protein Subunits, Hepatocytes, Mice
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