The DOI matches its Crossref record; 121 of the 121 references it cites were found in a registry or an index.
AMPK in Health and Disease
Abstract
The function and survival of all organisms is dependent on the dynamic control of energy metabolism, when energy demand is matched to energy supply. The AMP-activated protein kinase (AMPK) αβγ heterotrimer has emerged as an important integrator of signals that control energy balance through the regulation of multiple biochemical pathways in all eukaryotes. In this review, we begin with the discovery of the AMPK family and discuss the recent structural studies that have revealed the molecular basis for AMP binding to the enzyme's γ subunit. AMPK's regulation involves autoinhibitory features and phosphorylation of both the catalytic α subunit and the β-targeting subunit. We review the role of AMPK at the cellular level through examination of its many substrates and discuss how it controls cellular energy balance. We look at how AMPK integrates stress responses such as exercise as well as nutrient and hormonal signals to control food intake, energy expenditure, and substrate utilization at the whole body level. Lastly, we review the possible role of AMPK in multiple common diseases and the role of the new age of drugs targeting AMPK signaling.
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.
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
Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin
(2002) · New England Journal of Medicine · doi:10.1056/nejmoa012512 · Cited by 19,011
An obesity-associated gut microbiome with increased capacity for energy harvest
Turnbaugh, P. J., Ley, R. E., Mahowald, M. A., Magrini, V., Mardis, E. R., & Gordon, J. I. (2006) · Nature · doi:10.1038/nature05414 · Cited by 12,444
Tuomilehto, J., Lindström, J., Eriksson, J. G., Valle, T. T., Hämäläinen, H., Ilanne-Parikka, P., Keinänen-Kiukaanniemi, S., Laakso, M., Louheranta, A., Rastas, M., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejm200105033441801 · Cited by 10,873
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197
Inflammation and metabolic disorders
Hotamisligil, G. S. (2006) · Nature · doi:10.1038/nature05485 · Cited by 9,199
Human gut microbes associated with obesity
Ley, R. E., Turnbaugh, P. J., Klein, S., & Gordon, J. I. (2006) · Nature · doi:10.1038/4441022a · Cited by 8,785
The gut microbiota as an environmental factor that regulates fat storage
Bäckhed, F., Ding, H., Wang, T., Hooper, L. V., Koh, G. Y., Nagy, A., Semenkovich, C. F., & Gordon, J. I. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407076101 · Cited by 6,245
Obesity alters gut microbial ecology
Ley, R. E., Bäckhed, F., Turnbaugh, P., Lozupone, C. A., Knight, R. D., & Gordon, J. I. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504978102 · Cited by 6,176
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
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290
Cited by
Fatty acid–induced NLRP3-ASC inflammasome activation interferes with insulin signaling
Wen, H., Gris, D., Lei, Y., Jha, S., Zhang, L., Huang, M. T.-H., Brickey, W. J., & Ting, J. P.-Y. (2011) · Nature Immunology · doi:10.1038/ni.2022 · Cited by 1,698
Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network
Scarpulla, R. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.019 · Cited by 1,281
AMPK and SIRT1: a long-standing partnership?
Ruderman, N. B., Julia Xu, X., Nelson, L., Cacicedo, J. M., Saha, A. K., Lan, F., & Ido, Y. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00745.2009 · Cited by 903
Metformin, independent of AMPK, inhibits mTORC1 in a rag GTPase-dependent manner
Kalender, A., Selvaraj, A., Kim, S. Y., Gulati, P., Brûlé, S., Viollet, B., Kemp, B. E., Bardeesy, N., Dennis, P., Schlager, J. J., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.03.014 · Cited by 889
Self-citationSalminen, A., Hyttinen, J. M. T., & Kaarniranta, K. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0748-0 · Cited by 866
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
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
Lee, C., Zeng, J., Drew, B. G., Sallam, T., Martin-Montalvo, A., Wan, J., Kim, S.-J., Mehta, H., Hevener, A. L., de Cabo, R., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.009 · Cited by 715
Low-dose metformin targets the lysosomal AMPK pathway through PEN2
Ma, T., Tian, X., Zhang, B., Li, M., Wang, Y., Yang, C., Wu, J., Wei, X., Qu, Q., Yu, Y., et al. (2022) · Nature · doi:10.1038/s41586-022-04431-8 · Cited by 644
AMPK is a direct adenylate charge-regulated protein kinase
Oakhill, J. S., Steel, R., Chen, Z.-P., Scott, J. W., Ling, N., Tam, S., & Kemp, B. E. (2011) · Science · doi:10.1126/science.1200094 · Cited by 612
Self-citationSvensson, R. U., Parker, S. J., Eichner, L. J., Kolar, M. J., Wallace, M., Brun, S. N., Lombardo, P. S., Van Nostrand, J. L., Hutchins, A., Vera, L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4181 · Cited by 536
AMPK at the Nexus of Energetics and Aging
Burkewitz, K., Zhang, Y., & Mair, W. B. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.002 · Cited by 483
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-citationInflammaging: disturbed interplay between autophagy and inflammasomes
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2012) · Aging · doi:10.18632/aging.100444 · Cited by 453
Hoffman, N. J., Parker, B. L., Chaudhuri, R., Fisher-Wellman, K. H., Kleinert, M., Humphrey, S. J., Yang, P., Holliday, M., Trefely, S., Fazakerley, D. J., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.001 · Cited by 426
Vasamsetti, S. B., Karnewar, S., Kanugula, A. K., Thatipalli, A. R., Kumar, J. M., & Kotamraju, S. (2015) · Diabetes · doi:10.2337/db14-1225 · Cited by 397
O'Neill, H. M., Maarbjerg, S. J., Crane, J. D., Jeppesen, J., Jørgensen, S. B., Schertzer, J. D., Shyroka, O., Kiens, B., van Denderen, B. J., Tarnopolsky, M. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105062108 · Cited by 406
Self-citationLifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB
Mair, W., Morantte, I., Rodrigues, A. P. C., Manning, G., Montminy, M., Shaw, R. J., & Dillin, A. (2011) · Nature · doi:10.1038/nature09706 · Cited by 393
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
Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy
Myers, R. W., Guan, H.-P., Ehrhart, J., Petrov, A., Prahalada, S., Tozzo, E., Yang, X., Kurtz, M. M., Trujillo, M., Gonzalez Trotter, D., et al. (2017) · Science · doi:10.1126/science.aah5582 · Cited by 346
Leptin and the Central Nervous System Control of Glucose Metabolism
Morton, G. J., & Schwartz, M. W. (2011) · Physiological Reviews · doi:10.1152/physrev.00007.2010 · Cited by 338
“AMPK is a master sensor of cellular energy expressed in key metabolic tissues including liver, skeletal muscle, adipose tissue, and hypothalamus (179) and is activated when fuel availability is reduced, as during exercise, which in turn stimulates fat oxidation while increasing glucose uptake in muscle via an insulini…”
BackgroundKeeley, T. P., & Mann, G. E. (2019) · Physiological Reviews · doi:10.1152/physrev.00041.2017 · Cited by 329
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
Han, X., Tai, H., Wang, X., Wang, Z., Zhou, J., Wei, X., Ding, Y., Gong, H., Mo, C., Zhang, J., et al. (2016) · Aging Cell · doi:10.1111/acel.12446 · Cited by 302
The role of skeletal muscle mTOR in the regulation of mechanical load‐induced growth
Goodman, C. A., Frey, J. W., Mabrey, D. M., Jacobs, B. L., Lincoln, H. C., You, J., & Hornberger, T. A. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.218255 · Cited by 297
AMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286
Stephenne, X., Foretz, M., Taleux, N., van der Zon, G. C., Sokal, E., Hue, L., Viollet, B., & Guigas, B. (2011) · Diabetologia · doi:10.1007/s00125-011-2311-5 · Cited by 287
Fatigue and Fatigability in Older Adults
Eldadah, B. A. (2010) · PM&R · doi:10.1016/j.pmrj.2010.03.022 · Cited by 262
Autophagy in diabetic kidney disease: regulation, pathological role and therapeutic potential
Yang, D., Livingston, M. J., Liu, Z., Dong, G., Zhang, M., Chen, J.-K., & Dong, Z. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2639-1 · Cited by 252
Structure and Physiological Regulation of AMPK
Yan, Y., Zhou, X. E., Xu, H. E., & Melcher, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113534 · Cited by 254
The serine/threonine kinase ULK1 is a target of multiple phosphorylation events
Bach, M., Larance, M., James, D. E., & Ramm, G. (2011) · Biochemical Journal · doi:10.1042/bj20101894 · Cited by 233
Kitani, T., Ong, S.-G., Lam, C. K., Rhee, J.-W., Zhang, J. Z., Oikonomopoulos, A., Ma, N., Tian, L., Lee, J., Telli, M. L., et al. (2019) · Circulation · doi:10.1161/circulationaha.118.037357 · Cited by 200
AMPK activation: Role in the signaling pathways of neuroinflammation and neurodegeneration
Peixoto, C. A., Oliveira, W. H. D., Araújo, S. M. D. R., & Nunes, A. K. S. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.08.013 · Cited by 196
Phosphorylation of AMPK by upstream kinases is required for activity in mammalian cells
Willows, R., Sanders, M. J., Xiao, B., Patel, B. R., Martin, S. R., Read, J., Wilson, J. R., Hubbard, J., Gamblin, S. J., & Carling, D. (2017) · Biochemical Journal · doi:10.1042/bcj20170458 · Cited by 190
AMP-activated protein kinase: Also regulated by ADP?
Hardie, D. G., Carling, D., & Gamblin, S. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.004 · Cited by 187
Manna, P., Achari, A. E., & Jain, S. K. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.01.002 · Cited by 181
Ducommun, S., Deak, M., Sumpton, D., Ford, R. J., Núñez Galindo, A., Kussmann, M., Viollet, B., Steinberg, G. R., Foretz, M., Dayon, L., et al. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.008 · Cited by 167
Self-citationAMPK β1 Deletion Reduces Appetite, Preventing Obesity and Hepatic Insulin Resistance
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., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056762 · Cited by 175
Self-citationSantos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168
Activation of AMPKα2 in adipocytes is essential for nicotine-induced insulin resistance in vivo
Wu, Y., Song, P., Zhang, W., Liu, J., Dai, X., Liu, Z., Lu, Q., Ouyang, C., Xie, Z., Zhao, Z., et al. (2015) · Nature Medicine · doi:10.1038/nm.3826 · Cited by 169
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-citationThe Signaling Pathways Regulating NLRP3 Inflammasome Activation
Chen, M.-Y., Ye, X.-J., He, X.-H., & Ouyang, D.-Y. (2021) · Inflammation · doi:10.1007/s10753-021-01439-6 · Cited by 154
Hunter, R. W., Treebak, J. T., Wojtaszewski, J. F. P., & Sakamoto, K. (2011) · Diabetes · doi:10.2337/db10-1148 · Cited by 151
Exercise and mitochondrial dynamics: keeping in shape with ROS and AMPK
Trewin, A., Berry, B., & Wojtovich, A. (2018) · Antioxidants · doi:10.3390/antiox7010007 · Cited by 129
Activation of AMPK under Hypoxia: Many Roads Leading to Rome
Dengler, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072428 · 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
Nitric Oxide in Skeletal Muscle: Role on Mitochondrial Biogenesis and Function
Tengan, C., Rodrigues, G., & Godinho, R. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131217160 · Cited by 123
Chopra, I., Li, H. F., Wang, H., & Webster, K. A. (2012) · Diabetologia · doi:10.1007/s00125-011-2407-y · Cited by 116
Endurance factors improve hippocampal neurogenesis and spatial memory in mice
Kobilo, T., Yuan, C., & van Praag, H. (2011) · Learning & Memory · doi:10.1101/lm.2001611 · Cited by 114
Xu, Z., Huo, J., Ding, X., Yang, M., Li, L., Dai, J., Hosoe, K., Kubo, H., Mori, M., Higuchi, K., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08899-7 · Cited by 108
AMPK and the neuroendocrine regulation of appetite and energy expenditure
Stark, R., Ashley, S. E., & Andrews, Z. B. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.012 · Cited by 94
Salomäki, H., Vähätalo, L. H., Laurila, K., Jäppinen, N. T., Penttinen, A.-M., Ailanen, L., Ilyasizadeh, J., Pesonen, U., & Koulu, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056594 · Cited by 92
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
Oliveira, S. M., Zhang, Y.-H., Solis, R. S., Isackson, H., Bellahcene, M., Yavari, A., Pinter, K., Davies, J. K., Ge, Y., Ashrafian, H., et al. (2012) · Circulation Research · doi:10.1161/circresaha.111.259952 · Cited by 86
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
Self-citationA perspective on the determination of mitochondrial biogenesis
Miller, B. F., & Hamilton, K. L. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00578.2011 · Cited by 86
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
SIRT1 takes a backseat to AMPK in the regulation of insulin sensitivity by resveratrol
Fullerton, M. D., & Steinberg, G. R. (2010) · Diabetes · doi:10.2337/db09-1732 · Cited by 77
Self-citationGaccioli, F., White, V., Capobianco, E., Powell, T. L., Jawerbaum, A., & Jansson, T. (2013) · Biology of Reproduction · doi:10.1095/biolreprod.113.109702 · Cited by 76
AMPK is associated with the beneficial effects of antidiabetic agents on cardiovascular diseases
Lu, Q., Li, X., Liu, J., Sun, X., Rousselle, T., Ren, D., Tong, N., & Li, J. (2019) · Bioscience Reports · doi:10.1042/bsr20181995 · Cited by 69
Loss of Parkin impairs mitochondrial function and leads to muscle atrophy
Peker, N., Donipadi, V., Sharma, M., McFarlane, C., & Kambadur, R. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00064.2017 · Cited by 68
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
Shen, B., He, P.-J., & Shao, C.-L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0084610 · Cited by 66
Metformin inhibits ROS production by human M2 macrophages via the activation of AMPK
Nassif, R. M., Chalhoub, E., Chedid, P., Hurtado-Nedelec, M., Raya, E., Dang, P. M.-C., Marie, J.-C., & El-Benna, J. (2022) · Biomedicines · doi:10.3390/biomedicines10020319 · Cited by 63
Discovery of MK-8722: A systemic, direct pan-activator of amp-activated protein kinase
Feng, D., Biftu, T., Romero, F. A., Kekec, A., Dropinski, J., Kassick, A., Xu, S., Kurtz, M. M., Gollapudi, A., Shao, Q., et al. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00417 · Cited by 64
Kitada, M., Kume, S., Takeda-Watanabe, A., Tsuda, S.-I., Kanasaki, K., & Koya, D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.06.014 · Cited by 60
Lee, H.-K., Kwon, B., Lemere, C. A., de la Monte, S., Itamura, K., Ha, A. Y., & Querfurth, H. W. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161029 · Cited by 57
AMPK Knockdown in Placental Trophoblast Cells Results in Altered Morphology and Function
Carey, E. A. K., Albers, R. E., Doliboa, S. R., Hughes, M., Wyatt, C. N., Natale, D. R. C., & Brown, T. L. (2014) · Stem Cells and Development · doi:10.1089/scd.2014.0092 · Cited by 56
Shah, S. Z. A., Zhao, D., Hussain, T., & Yang, L. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.09.004 · Cited by 55
PKC-Dependent Human Monocyte Adhesion Requires AMPK and Syk Activation
Chang, M.-Y., Huang, D.-Y., Ho, F.-M., Huang, K.-C., & Lin, W.-W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040999 · Cited by 54
Kahl, K. G., Stapel, B., & Frieling, H. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2018.09.004 · Cited by 47
Utilizing small nutrient compounds as enhancers of exercise-induced mitochondrial biogenesis
Craig, D. M., Ashcroft, S. P., Belew, M. Y., Stocks, B., Currell, K., Baar, K., & Philp, A. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00296 · Cited by 45
AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy
Dohmen, M., Krieg, S., Agalaridis, G., Zhu, X., Shehata, S. N., Pfeiffenberger, E., Amelang, J., Bütepage, M., Buerova, E., Pfaff, C. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14812-0 · Cited by 40
Han, J., Yang, N., Zhang, F., Zhang, C., Liang, F., Xie, W., & Chen, W. (2015) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2015.05.016 · Cited by 39
Kodiha, M., Salimi, A., Wang, Y. M., & Stochaj, U. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088087 · Cited by 29
Current Perspectives on Nonalcoholic Fatty Liver Disease in Women with Polycystic Ovary Syndrome
Wang, D., & He, B. (2022) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s362424 · Cited by 28
Hepatic Glucose Intolerance Precedes Hepatic Steatosis in the Male Aromatase Knockout (ArKO) Mouse
Van Sinderen, M. L., Steinberg, G. R., Jørgensen, S. B., To, S. Q., Knower, K. C., Clyne, C. D., Honeyman, J., Chow, J. D., Herridge, K. A., Jones, M. E. E., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087230 · Cited by 26
Self-citationAnsari, P., Khan, J. T., Choudhary, S., Reberio, A. D., Kumar, S., Seidel, V., Abdel-Wahab, Y. H. A., & Flatt, P. R. (2024) · doi:10.20944/preprints202408.1739.v1 · Cited by 89
Metabolic regulation by biomaterials in osteoblast
Kang, Z., Wu, B., Zhang, L., Liang, X., Guo, D., Yuan, S., & Xie, D. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1184463 · Cited by 15
Buniam, J., Chansela, P., Weerachayaphorn, J., & Saengsirisuwan, V. (2023) · Biomedicines · doi:10.3390/biomedicines11072071 · Cited by 9
Black, M. N., Wilkinson, J. A., Webb, E. K., Kamal, M., Bahniwal, R., McGlory, C., Phillips, S. M., & Devries, M. C. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00878.2019 · Cited by 6
Metadata
- Authors
- Steinberg, G. R., & Kemp, B. E.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2009-07
- Volume
- 89
- Issue
- 3
- Pages
- 1025-1078
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2150551377
- Cited by
- 1,637
- References
- 121
- FWCI
- 5.07
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
