Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism
Open accessAbstract
The AMP-activated protein kinase (AMPK) is a sensor of cellular energy status, and a regulator of energy balance at both the cellular and whole body levels. Although ubiquitously expressed, its function is best understood in skeletal muscle. AMPK contains sites that reversibly bind AMP or ATP, with an increase in cellular AMP:ATP ratio (signalling a fall in cellular energy status) switching on the kinase. In muscle, AMPK activation is therefore triggered by sustained contraction, and appears to be particularly important in the metabolic changes that occur in the transition from resistance to endurance exercise. Once activated, AMPK switches on catabolic processes that generate ATP, while switching off energy-requiring processes not essential in the short term. Thus, it acutely activates glucose uptake (by promoting translocation of the transporter GLUT4 to the membrane) and fatty acid oxidation, while switching off glycogen synthesis and protein synthesis (the later via inactivation of the mammalian target-of-rapamycin pathway). Prolonged AMPK activation also causes some of the chronic adaptations to endurance exercise, such as increased GLUT4 expression and mitochondrial biogenesis. AMPK contains a glycogen-binding domain that causes a sub-fraction to bind to the surface of the glycogen particle, and it can inhibit glycogen synthesis by phosphorylating glycogen synthase. We have shown that AMPK is inhibited by exposed non-reducing ends in glycogen. We are working on the hypothesis that this ensures that glycogen synthesis is rapidly activated when glycogen becomes depleted after exercise, but is switched off again as soon as glycogen stores are replenished.
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
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?
AMPK is a key mediator of the adaptation to endurance exercise, particularly in skeletal muscle.
“Therefore, it comes as no surprise that AMPK is a key mediator of the adaptation to endurance exercise, particularly in skeletal muscle (54).”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [54]
Prolonged AMPK activation can lead to a chronic adaptation to endurance exercise, like mitochondrial biogenesis and increased GLUT4 expression.
“Prolonged AMPK activation can lead to a chronic adaptation to endurance exercise, like mitochondrial biogenesis and increased GLUT4 expression [60].”
From Regulation of Energy Substrate Metabolism in Endurance Exercise (2021) · cites this paper as [60]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · see citing works
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 · see citing works
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238 · see citing works
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914 · see citing works
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849 · see citing works
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works
Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176 · see citing works
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491 · see citing works
AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
Hardie, D. G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2249 · Cited by 2,207 · see citing works
Self-citationMitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070 · see citing works
Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053 · see citing works
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 · see citing works
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 1,666 · see citing works
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 · see citing works
AMP-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 · see citing works
The Mitochondrial Carnitine Palmitoyltransferase System — From Concept to Molecular Analysis
McGarry, J. D., & Brown, N. F. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00001.x · Cited by 1,616 · cited 5× · see citing works
“Carnitine-palmitoyl transferase-1 is required for the uptake of fatty acids into mitochondria, and is inhibited in resting muscle by the malonyl-CoA produced by ACC2((48)).”
BackgroundInfluentialHawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.009 · Cited by 1,589 · see citing works
Self-citationTHE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?
Hardie, D. G., Carling, D., & Carlson, M. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.821 · Cited by 1,436 · see citing works
Self-citationWoods, A., Dickerson, K., Heath, R. B., Hong, S. P., Momcilovic, M., Johnstone, S. R., Carlson, M., & Carling, D. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.005 · Cited by 1,395 · see citing works
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 · see citing works
Self-citationMu, J., Brozinick, J. T., Valladares, O., Bucan, M., & Birnbaum, M. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00251-9 · Cited by 924 · see citing works
Carey, A. L., Steinberg, G. R., Macaulay, S. L., Thomas, W. G., Holmes, A. G., Ramm, G., Prelovsek, O., Hohnen-Behrens, C., Watt, M. J., James, D. E., et al. (2006) · Diabetes · doi:10.2337/db05-1404 · Cited by 898 · see citing works
Bolster, D. R., Crozier, S. J., Kimball, S. R., & Jefferson, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200171200 · Cited by 851 · see citing works
Adiponectin Stimulates AMP-Activated Protein Kinase in the Hypothalamus and Increases Food Intake
Kubota, N., Yano, W., Kubota, T., Yamauchi, T., Itoh, S., Kumagai, H., Kozono, H., Takamoto, I., Okamoto, S., Shiuchi, T., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.06.003 · Cited by 844 · see citing works
Marsin, A.-S., Bertrand, L., Rider, M. H., Deprez, J., Beauloye, C., Vincent, M. F., den Berghe, G. V., Carling, D., & Hue, L. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00742-9 · Cited by 818 · see citing works
Winder, W. W., & Hardie, D. G. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.270.2.e299 · Cited by 799 · see citing works
Self-citationUse of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation
Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773 · see citing works
Self-citationAMP-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 756 · see citing works
Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754 · see citing works
Self-citationRussell, R. R., Li, J., Coven, D. L., Pypaert, M., Zechner, C., Palmeri, M., Giordano, F. J., Mu, J., Birnbaum, M. J., & Young, L. H. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19297 · Cited by 738 · see citing works
Baar, K., & Esser, K. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.1.c120 · Cited by 726 · see citing works
Apfeld, J., O'Connor, G., McDonagh, T., DiStefano, P. S., & Curtis, R. (2004) · Genes & Development · doi:10.1101/gad.1255404 · Cited by 643 · see citing works
Carling, D., Zammit, V. A., & Hardie, D. G. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80292-2 · Cited by 599 · see citing works
Self-citationStructural basis for AMP binding to mammalian AMP-activated protein kinase
Xiao, B., Heath, R., Saiu, P., Leiper, F. C., Leone, P., Jing, C., Walker, P. A., Haire, L., Eccleston, J. F., Davis, C. T., et al. (2007) · Nature · doi:10.1038/nature06161 · Cited by 591 · see citing works
Kudo, N., Barr, A., Barr, R. L., Desai, S. S., & Lopaschuk, G. D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17513 · Cited by 565 · see citing works
Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
Sakamoto, K., McCarthy, A., Smith, D. P., Green, K. A., Hardie, D. G., Ashworth, A., & Alessi, D. R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600667 · Cited by 544 · see citing works
Self-citationKim, M., Park, J., NamKoong, C., Jang, P., Ryu, J., Song, H.-S., Yun, J.-Y., Nam‐Goong, I. S., Ha, J., Park, I.-S., et al. (2004) · Nature Medicine · doi:10.1038/nm1061 · Cited by 522 · see citing works
AMPK is essential for energy homeostasis regulation and glucose sensing by POMC and AgRP neurons
Claret, M., Smith, M. A., Batterham, R. L., Selman, C., Choudhury, A. I., Fryer, L. G. D., Clements, M., Al‐Qassab, H., Heffron, H., Xu, A. W., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31516 · Cited by 506 · see citing works
Suter, M., Riek, U., Tuerk, R. D., Schlattner, U., Wallimann, T., & Neumann, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606357200 · Cited by 473 · see citing works
Kola, B., Hubina, E., Tucci, S. A., Kirkham, T. C., García, E., Mitchell, S. E., Williams, L. M., Hawley, S. A., Hardie, D. G., Grossman, A. B., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500175200 · Cited by 468 · see citing works
Self-citationAMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
McGee, S. L., van Denderen, B. J. W., Howlett, K. F., Mollica, J., Schertzer, J. D., Kemp, B. E., & Hargreaves, M. (2008) · Diabetes · doi:10.2337/db07-0843 · Cited by 455 · see citing works
Glycogen Synthetase Activity in Skeletal Muscle
Danforth, W. H. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45214-8 · Cited by 435 · see citing works
The Glycogen-Binding Domain on the AMPK β Subunit Allows the Kinase to Act as a Glycogen Sensor
McBride, A., Ghilagaber, S., Nikolaev, A., & Hardie, D. G. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.11.008 · Cited by 432 · see citing works
Self-citationMiller, E. J., Li, J., Leng, L., McDonald, C., Atsumi, T., Bucala, R., & Young, L. H. (2008) · Nature · doi:10.1038/nature06504 · Cited by 429 · see citing works
AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen
Polekhina, G., Gupta, A., Michell, B. J., van Denderen, B., Murthy, S., Feil, S. C., Jennings, I. G., Campbell, D. J., Witters, L. A., Parker, M. W., et al. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00292-6 · Cited by 423 · see citing works
Salt, I. P., JOHNSON, G., Ashcroft, S. J. H., & Hardie, D. G. (1998) · Biochemical Journal · doi:10.1042/bj3350533 · Cited by 408 · see citing works
Self-citationAMP-Activated Protein Kinase as a Drug Target
Hardie, D. G. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105304 · Cited by 405 · see citing works
Self-citationLochhead, P. A., Salt, I. P., Walker, K. S., Hardie, D. G., & Sutherland, C. D. (2000) · Diabetes · doi:10.2337/diabetes.49.6.896 · Cited by 391 · see citing works
Self-citationMusi, N., Fujii, N., Hirshman, M. F., Ekberg, I., Fröberg, S., Ljungqvist, O., Thorell, A., & Goodyear, L. J. (2001) · Diabetes · doi:10.2337/diabetes.50.5.921 · Cited by 371 · cited 1× · see citing works
“In insulinresistant individuals, insulin-dependent activation of protein kinase B is defective, but the mechanism by which contraction stimulates glucose uptake via AMPK remains unaffected((46)).”
BackgroundHudson, E. R., Pan, D. A., James, J., Lucocq, J. M., Hawley, S. A., Green, K. A., Baba, O., Terashima, T., & Hardie, D. G. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00249-5 · Cited by 332 · see citing works
Self-citationmTOR, translational control and human disease
Tee, A. R., & Blenis, J. (2005) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2004.11.005 · Cited by 320 · see citing works
Carling, D., & Grahame Hardie, D. (1989) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(89)90014-1 · Cited by 296 · see citing works
Self-citationRegulation of muscle GLUT-4 transcription by AMP-activated protein kinase
Zheng, D., MacLean, P. S., Pohnert, S. C., Knight, J. B., Olson, A. L., Winder, W. W., & Dohm, G. L. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.91.3.1073 · Cited by 292 · see citing works
CNTF reverses obesity-induced insulin resistance by activating skeletal muscle AMPK
Watt, M. J., Dzamko, N. L., Thomas, W. G., Rose‐John, S., Ernst, M., Carling, D., Kemp, B. E., Febbraio, M. A., & Steinberg, G. R. (2006) · Nature Medicine · doi:10.1038/nm1383 · Cited by 275 · see citing works
Xavier, G. D. S., Leclerc, I., Váradi, A., Tsuboi, T., MOULE, S. K., & Rutter, G. A. (2003) · Biochemical Journal · doi:10.1042/bj20021812 · Cited by 257 · see citing works
Jørgensen, S. B., Nielsen, J. N., Birk, J. B., Olsen, G. S., Viollet, B., Andreelli, F., Schjerling, P., Vaulont, S., Hardie, D. G., Hansen, B. F., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.12.3074 · Cited by 241 · see citing works
Self-citationWinder, W. W., Wilson, H. A., Hardie, D. G., Rasmussen, B. B., Hutber, C. A., Call, G. B., Clayton, R. D., Conley, L. M., Yoon, S., & Zhou, B. (1997) · Journal of Applied Physiology · doi:10.1152/jappl.1997.82.1.219 · Cited by 237 · see citing works
Self-citationComplementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
Chen, S., Murphy, J. E., Toth, R. L., Campbell, D. G., MORRICE, N. A., & MacKintosh, C. (2007) · Biochemical Journal · doi:10.1042/bj20071114 · Cited by 207 · see citing works
Optimization of molecular design in the evolution of metabolism: the glycogen molecule
Meléndez‐Hevia, E., Waddell, T. K., & Shelton, E. D. (1993) · Biochemical Journal · doi:10.1042/bj2950477 · Cited by 187 · see citing works
The AMP-activated protein kinase: a multisubstrate regulator of lipid metabolism
Hardie, D. G., Carling, D., & Sim, A. T. R. (1989) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(89)90084-4 · Cited by 178 · see citing works
Self-citationNarbonne, P., & Roy, R. (2006) · Development · doi:10.1242/dev.02232 · Cited by 175 · see citing works
McCrimmon, R. J., Shaw, M., Fan, X., Cheng, H. M., Ding, Y., Vella, M. C., Zhou, L., McNay, E. C., & Sherwin, R. S. (2007) · Diabetes · doi:10.2337/db07-0837 · Cited by 172 · see citing works
Pehmøller, C., Treebak, J. T., Birk, J. B., Chen, S., MacKintosh, C., Hardie, D. G., Richter, E. A., & Wojtaszewski, J. F. P. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00115.2009 · Cited by 171 · see citing works
Self-citationKim, W., Botchkarev, A. E., Salvador, A., Popovici, G., Tang, H., & Morkoç, H. (1997) · Journal of Applied Physics · doi:10.1063/1.365801 · Cited by 168 · see citing works
Snf1‐related protein kinase 1 is needed for growth in a normal day–night light cycle
Thelander, M., Olsson, T., & Ronne, H. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600182 · Cited by 155 · see citing works
McCrimmon, R. J., Fan, X., Ding, Y., Zhu, W., Jacob, R. J., & Sherwin, R. S. (2004) · Diabetes · doi:10.2337/diabetes.53.8.1953 · Cited by 148 · see citing works
Aschenbach, W. G., Suzuki, Y., Breeden, K., Prats, C., Hirshman, M. F., Dufresne, S. D., Sakamoto, K., Vilardo, P. G., Steele, M., Kim, J.-H., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105518200 · Cited by 106 · see citing works
Steinberg, G. R., Watt, M. J., Fam, B. C., Proietto, J., Andrikopoulos, S., Allen, A. M., Febbraio, M. A., & Kemp, B. E. (2006) · Endocrinology · doi:10.1210/en.2005-1587 · Cited by 101 · see citing works
Rose, A. J., Bisiani, B., Vistisen, B., Kiens, B., & Richter, E. A. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90806.2008 · Cited by 65 · see citing works
Bendayan, M., London, I. G., Kemp, B. E., Hardie, D. G., Ruderman, N. B., & Prentki, M. (2009) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2009.954016 · Cited by 41 · see citing works
Self-citationAMP-activated protein kinase and hypoxic pulmonary vasoconstriction
Robertson, T. P., Mustard, K. J. W., Lewis, T. H. J., Clark, J. H., Wyatt, C. N., Blanco, E. A., Peers, C., Hardie, D. G., & Evans, A. M. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.07.035 · Cited by 40 · see citing works
Self-citationEVANS, A. M., Mustard, K. J. W., Wyatt, C. N., Dipp, M., Kinnear, N. P., & Hardie, D. G. (2006) · Springer eBooks · doi:10.1007/0-387-31311-7_22 · Cited by 13 · see citing works
Self-citationKey Roles for AMP-activated Protein Kinase in the Function of the Carotid Body?
Wyatt, C. N., Pearson, S. A., Kumar, P., Peers, C., Hardie, D. G., & Evans, A. M. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-73693-8_11 · Cited by 8 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
AMPK activators: mechanisms of action and physiological activities
Kim, J., Yang, G., Kim, Y., Kim, J., & Ha, J. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.16 · Cited by 817 · see citing works
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 496 · see citing works
Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism
Liemburg-Apers, D. C., Willems, P. H. G. M., Koopman, W. J. H., & Grefte, S. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1520-y · Cited by 391 · see citing works
Jin, Q., Cheng, J. G., Liu, Y., Wu, J. H., Wang, X., Wei, S., Zhou, X., Qin, Z., Jia, J., & Zhen, X. (2014) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2014.03.003 · Cited by 294 · see citing works
White, J. P., Baynes, J. W., Welle, S. L., Kostek, M. C., Matesic, L. E., Sato, S., & Carson, J. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024650 · Cited by 260 · see citing works
“AMPK is activated by low cellular energy status and also muscle contraction [22].”
BNip3 Regulates Mitochondrial Function and Lipid Metabolism in the Liver
Glick, D., Zhang, W., Beaton, M., Marsboom, G., Gruber, M., Simon, M. C., Hart, J., Dorn, G. W., Brady, M. J., & Macleod, K. F. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00167-12 · Cited by 251 · see citing works
Testosterone regulation of Akt/mTORC1/FoxO3a signaling in skeletal muscle
White, J. P., Gao, S., Puppa, M., Sato, S., Welle, S. L., & Carson, J. A. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.10.019 · Cited by 250 · see citing works
NAD+/NADH and skeletal muscle mitochondrial adaptations to exercise
White, A. T., & Schenk, S. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00054.2012 · Cited by 193 · see citing works
Exercise and regulation of carbohydrate metabolism
Mul, J. D., Stanford, K. I., Hirshman, M. F., & Goodyear, L. J. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.07.020 · Cited by 151 · see citing works
Kim, M., Hur, H. J., Kwon, D. Y., & Hwang, J. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.03.013 · Cited by 138 · see citing works
The regulation of autophagy during exercise in skeletal muscle
Vainshtein, A., & Hood, D. A. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00550.2015 · Cited by 132 · see citing works
AMPK agonist AICAR improves cognition and motor coordination in young and aged micePreprint
Kobilo, T., Guerrieri, D., Zhang, Y., Collica, S. C., Becker, K. G., & van Praag, H. (2014) · Learning & Memory · doi:10.1101/lm.033332.113 · Cited by 128 · see citing works
Molecular Mechanisms of Muscle Plasticity with Exercise
Hoppeler, H. H., Baum, O., Lurman, G. J., & Mueller, M. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100042 · Cited by 120 · see citing works
Reyes, N. L., Banks, G. B., Tsang, M., Margineantu, D. H., Gu, H., Djukovic, D., Chan, J. I. S., Torres, M., Liggitt, H. D., Hirenallur-Shanthappa, D. K., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413021112 · Cited by 116 · see citing works
Zhao, X., Petursson, F., Viollet, B., Lotz, M., Terkeltaub, R. A., & Liu‐Bryan, R. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38791 · Cited by 114 · see citing works
Vandoorne, T., Smet, S. D., Ramaekers, M., Thienen, R. V., Bock, K. D., Clarke, K., & Hespel, P. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00310 · Cited by 112 · see citing works
Regulation of Energy Substrate Metabolism in Endurance Exercise
Alghannam, A. F., Ghaith, M. M., & Alhussain, M. H. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18094963 · Cited by 104 · see citing works
“Prolonged AMPK activation can lead to a chronic adaptation to endurance exercise, like mitochondrial biogenesis and increased GLUT4 expression [60].”
BackgroundHe, J., Chen, L.-X., & Li, H. (2019) · Fitoterapia · doi:10.1016/j.fitote.2019.02.033 · Cited by 102 · see citing works
Mo, M., Zhang, Z., Wang, X., Shen, W., Zhang, L., & Lin, S. (2023) · Frontiers in Veterinary Science · doi:10.3389/fvets.2023.1284551 · Cited by 102 · see citing works
Synthesis and Mechanism of Hypoglycemic Activity of Benzothiazole Derivatives
Meltzer-Mats, E., Babai-Shani, G., Pasternak, L., Uritsky, N., Getter, T., Viskind, O., Eckel, J., Cerasi, E., Senderowitz, H., Sasson, S., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4001488 · Cited by 95 · see citing works
Temperature and the Cardiovascular System
Eliason, E. J., & Anttila, K. (2017) · Fish physiology · doi:10.1016/bs.fp.2017.09.003 · Cited by 92 · see citing works
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 86 · see citing works
Yamashita, Y., Wang, L., Nanba, F., Ito, C., Toda, T., & Ashida, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161704 · Cited by 83 · see citing works
Brandauer, J., Agerholm, M., Kellezi, H., Risis, S., Frøsig, C., Vienberg, S. G., & Treebak, J. T. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00085 · Cited by 82 · see citing works
Siddique, M. M., Li, Y., Wang, L., Ching, J., Mal, M., Ilkayeva, O., Wu, Y., Bay, B., & Summers, S. A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00226-13 · Cited by 82 · see citing works
Chen, Z., Farrell, A. P., Matala, A. R., & Narum, S. R. (2017) · Molecular Ecology · doi:10.1111/mec.14475 · Cited by 82 · see citing works
Jost, J., Подольский, С. А., & Frederich, M. (2011) · Marine Ecology Progress Series · doi:10.3354/meps09379 · Cited by 80 · see citing works
Physical Activity and Telomere Biology: Exploring the Link with Aging-Related Disease Prevention
Ludlow, A. T., & Roth, S. M. (2011) · Journal of Aging Research · doi:10.4061/2011/790378 · Cited by 79 · see citing works
Burke, J. D., Platanias, L. C., & Fish, E. N. (2014) · Journal of Virology · doi:10.1128/jvi.02649-13 · Cited by 78 · see citing works
Ruggieri, S., Orsomando, G., Sorci, L., & Raffaelli, N. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.02.021 · Cited by 71 · see citing works
Judson, R. N., Gray, S. R., Walker, C. A., Carroll, A. M., Itzstein, C., Lionikas, A., Zammit, P. S., Bari, C. D., & Wackerhage, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059622 · Cited by 70 · see citing works
Anttila, K., Casselman, M. T., Schulte, P. M., & Farrell, A. P. (2013) · Physiological and Biochemical Zoology · doi:10.1086/669265 · Cited by 68 · see citing works
Benziane, B., Björnholm, M., Pirkmajer, S., Austin, R. L., Kotova, O., Viollet, B., Zierath, J. R., & Chibalin, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.331926 · Cited by 66 · see citing works
Bakker, A. D., & Jaspers, R. T. (2015) · Current Osteoporosis Reports · doi:10.1007/s11914-015-0264-1 · Cited by 64 · see citing works
Wijngaarden, M. A., van der Zon, G. C., van Dijk, K. W., Pijl, H., & Guigas, B. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00008.2013 · Cited by 63 · see citing works
Érdi, B., Nagy, P., Zvara, Á., Varga, Á., Pircs, K., Ménesi, D., Puskás, L. G., & Juhász, G. (2012) · Autophagy · doi:10.4161/auto.20069 · Cited by 60 · see citing works
Control strategies in systemic metabolism
Ye, J. J., & Medzhitov, R. M. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0118-8 · Cited by 60 · see citing works
Hsu, W.-H., Lee, B., Chang, Y.-Y., Hsu, Y.-W., & Pan, T. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.07.004 · Cited by 57 · see citing works
Involvement of AMPK in regulating slow-twitch muscle atrophy during hindlimb unloading in mice
Egawa, T., Goto, A., Ohno, Y., Yokoyama, S., Ikuta, A., Suzuki, M., Sugiura, T., Ohira, Y., Yoshioka, T., Hayashi, T., et al. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00165.2015 · Cited by 56 · see citing works
Roberts, F. L., & Markby, G. R. (2021) · Cells · doi:10.3390/cells10102639 · Cited by 53 · see citing works
Braun, K. A., Vaga, S., Dombek, K. M., Fang, F., Palmisano, S., Aebersold, R. H., & Young, E. T. (2014) · Science Signaling · doi:10.1126/scisignal.2005000 · Cited by 53 · see citing works
Daidzein alleviates cisplatin‐induced muscle atrophy by regulating Glut4/ AMPK / FoxO pathway
Zhang, H., Chi, M., Chen, L., Sun, X., Wan, L., Yang, Q., & Guo, C. (2021) · Phytotherapy Research · doi:10.1002/ptr.7132 · Cited by 52 · see citing works
The Hippo signal transduction network for exercise physiologists
Gabriel, B. M., Hamilton, D. L., Tremblay, A. M., & Wackerhage, H. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01076.2015 · Cited by 48 · see citing works
Promotion of insulin-induced glucose uptake in C2C12 myotubes by osteocalcin
Tsuka, S., Aonuma, F., Higashi, S., Ohsumi, T., Nagano, K., Mizokami, A., Kawakubo‐Yasukochi, T., Masaki, C., Hosokawa, R., Hirata, M., et al. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.123 · Cited by 48 · see citing works
AMP-activated protein kinase regulation of kidney tubular transport
Pastor‐Soler, N. M., & Hallows, K. R. (2012) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e3283562390 · Cited by 48 · see citing works
Bhansali, S., Bhansali, A., & Dhawan, V. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14141 · Cited by 45 · see citing works
Akebia saponin D alleviates hepatic steatosis through BNip3 induced mitophagy
Gong, L., Yang, S. T., Zhang, W., Han, F.-F., Lv, Y., Wan, Z., Liu, H., Jia, Y., Xuan, L., & Liu, L. (2017) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2017.11.007 · Cited by 44 · see citing works
Torre-Villalvazo, I., Alemán, G., Valle‐Rios, R., & Noriega, L. G. (2019) · Nutrition Research · doi:10.1016/j.nutres.2019.06.006 · Cited by 44 · see citing works
Autophagy, Myocardial Protection, and the Metabolic Syndrome
Giricz, Z., Mentzer, R. M., & Gottlieb, R. A. (2012) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e318256ce10 · Cited by 43 · see citing works
Cardiac contraction-induced GLUT4 translocation requires dual signaling input
Luiken, J. J. F. P., Glatz, J. F. C., & Neumann, D. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.06.002 · Cited by 43 · see citing works
Yamada, T., Ivarsson, N., Hernández, A., Fahlström, A., Cheng, A. J., Zhang, S., Bruton, J. D., Ulfhake, B., & Westerblad, H. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.240077 · Cited by 41 · see citing works
Egawa, T., Ohno, Y., Goto, A., Ikuta, A., Suzuki, M., Ohira, T., Yokoyama, S., Sugiura, T., Ohira, Y., Yoshioka, T., et al. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00495.2013 · Cited by 41 · see citing works
The effect of exercise induced cytokines on insulin stimulated glucose transport in C2C12 cells
Gray, S. R., & Kamolrat, T. (2011) · Cytokine · doi:10.1016/j.cyto.2011.04.019 · Cited by 40 · see citing works
Abadi, A., Crane, J. D., Ogborn, D. I., Hettinga, B. P., Akhtar, M., Stokl, A., MacNeil, L., Safdar, A., & Tarnopolsky, M. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060722 · Cited by 40 · see citing works
Wijngaarden, M. A., Bakker, L. E. H., van der Zon, G. C., Hoen, P. A. C. ’., van Dijk, K. W., Jazet, I. M., Pijl, H., & Guigas, B. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00215.2014 · Cited by 38 · see citing works
Kuo, Y.-T., Lin, C., Kuo, H.-T., Hung, J., Liu, C., Jassey, A., Yen, M., Wu, S.-J., & Lin, L. (2018) · Journal of Food and Drug Analysis · doi:10.1016/j.jfda.2018.07.002 · Cited by 37 · see citing works
Increasing effect of Tangzhiqing formula on IRS-1-dependent PI3K/AKT signaling in muscle
Gao, J., Li, J., An, Y., Liu, X., Qian, Q., Wu, Y., Zhang, Y., & Wang, T. (2014) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-14-198 · Cited by 36 · see citing works
Tang, J., He, A., Yan, H., Jia, G., Liu, G., Chen, X., Cai, J., Tian, G., Shang, H., & Zhao, H. Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-29012-6 · Cited by 36 · see citing works
Young, E. T., Zhang, C., Shokat, K. M., Parua, P. K., & Braun, K. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380147 · Cited by 36 · see citing works
Zhao, P., Alam, M. B., Lee, S.-H., Kim, Y., Lee, S., An, H., Choi, H.-J., Son, H.-U., Park, C., Kim, H., et al. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/6091923 · Cited by 35 · see citing works
The Regulation of Lipokines by Environmental Factors
Hernández‐Saavedra, D., & Stanford, K. I. (2019) · Nutrients · doi:10.3390/nu11102422 · Cited by 34 · see citing works
The Role of Fatty Acid Oxidation in the Metabolic Reprograming of Activated T-Cells
Byersdorfer, C. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00641 · Cited by 32 · see citing works
Factors Influencing AMPK Activation During Cycling Exercise: A Pooled Analysis and Meta-Regression
Rothschild, J. A., Islam, H., Bishop, D. J., Kilding, A. E., Stewart, T. I., & Plews, D. J. (2021) · Sports Medicine · doi:10.1007/s40279-021-01610-x · Cited by 32 · see citing works
The Functional Logic of Cytosolic 5’-Nucleotidases.
Ipata, P. L., & Balestri, F. (2013) · Current Medicinal Chemistry · doi:10.2174/0929867311320340002 · Cited by 32 · see citing works
Effects of H2O2 on Insulin Signaling the Glucose Transport System in Mammalian Skeletal Muscle
Henriksen, E. J. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405881-1.00016-1 · Cited by 31 · see citing works
Lettieri‐Barbato, D., Baldelli, S., Pagliei, B., Aquilano, K., & Ciriolo, M. R. (2012) · International Journal of Cell Biology · doi:10.1155/2012/759583 · Cited by 31 · see citing works
AMPK activation—protean potential for boosting healthspan
McCarty, M. F. (2013) · AGE · doi:10.1007/s11357-013-9595-y · Cited by 30 · see citing works
Elahi, D., Angeli, F. S., Vakilipour, A., Carlson, O. D., Tomás, E., Egan, J. M., Habener, J. F., & Shannon, R. P. (2014) · Peptides · doi:10.1016/j.peptides.2014.06.004 · Cited by 29 · see citing works
AMP-activated protein kinase controls lipid and lactose synthesis in bovine mammary epithelial cells
Huang, J., Guesthier, M.-A., & Burgos, S. A. (2019) · Journal of Dairy Science · doi:10.3168/jds.2019-16343 · Cited by 28 · see citing works
Zhang, B., Liu, N., He, Z., Song, P., Hao, M., Xie, Y., Li, J., Liu, R., & Sun, Z. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.631194 · Cited by 27 · see citing works
Obici, S., Magrisso, I. J., Ghazarian, A. S., Shirazian, A., Miller, J. R., Loyd, C., Begg, D. P., Carhuatanta, K. A. K., Haas, M. K., Davis, J. F., et al. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.07.003 · Cited by 25 · see citing works
Vigelsø, A., Gram, M., Dybboe, R., Kuhlman, A. B., Prats, C., Greenhaff, P. L., Constantin‐Teodosiu, D., Birk, J. B., Wojtaszewski, J. F. P., Dela, F., et al. (2016) · The Journal of Physiology · doi:10.1113/jp271712 · Cited by 24 · see citing works
Song, X., Jin, C., Wu, R., Wang, Y., & Wang, X. Q. (2025) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-025-01279-6 · Cited by 24 · see citing works
Proeyen, K. V., Szlufcik, K., Nielens, H., Deldicque, L., Dyck, R. V., Ramaekers, M., & Hespel, P. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01459.2010 · Cited by 24 · see citing works
The adipokine zinc-α2-glycoprotein activates AMP kinase in human primary skeletal muscle cells
Eckardt, K., Schober, A., Platzbecker, B., Mráček, T., Bing, C., Trayhurn, P., & Eckel, J. (2011) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2011.560950 · Cited by 23 · see citing works
Shanak, S., Bassalat, N., Barghash, A., Kadan, S., Ardah, M., & Zaid, H. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/2832889 · Cited by 22 · see citing works
Miyatake, S., Manabe, Y., Inagaki, A., Furuichi, Y., Takagi, M., Taoka, M., Isobe, T., Hirota, K., & FUJII, N. L. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.089 · Cited by 22 · see citing works
Disorders of the Endocrine System
Reed, S. M., Bayly, W. M., & Sellon, D. C. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-44329-6.00016-4 · Cited by 21 · see citing works
Terada, T., Eshghi, S. R. T., Liubaoerjijin, Y., Kennedy, M. D., Myette‐Côté, É., Fletcher, K., & Boulé, N. G. (2019) · The Journal of Sports Medicine and Physical Fitness · doi:10.23736/s0022-4707.18.08281-6 · Cited by 21 · see citing works
Piwkowska, A., Rogacka, D., Angielski, S., & Jankowski, M. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.10.033 · Cited by 19 · see citing works
Chen, J., You, L., & Luo, R. (2022) · Food Science & Nutrition · doi:10.1002/fsn3.2780 · Cited by 17 · see citing works
Glucose deprivation attenuates sortilin levels in skeletal muscle cells
Ariga, M., Yoneyama, Y., Fukushima, T., Ishiuchi, Y., Ishii, T., Sato, H., Hakuno, F., Nedachi, T., & Takahashi, S. (2016) · Endocrine Journal · doi:10.1507/endocrj.ej16-0319 · Cited by 16 · see citing works
Yang, L., Xie, L., Li, M., Miao, Y., Yang, J., Chen, S., Ma, X., & Xie, P. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1520669 · Cited by 15 · see citing works
Pallottini, V., Colardo, M., Tonini, C., Martella, N., Strimpakos, G., Colella, B., Tirassa, P., Bartolomeo, S. D., & Segatto, M. (2020) · Cells · doi:10.3390/cells9102232 · Cited by 15 · see citing works
Tarawan, V. M., Gunadi, J. W., Setiawan, S., Lesmana, R., Goenawan, H., Meilina, D. E., Sipayung, J. A., Wargasetia, T. L., Widowati, W., Limyati, Y., et al. (2019) · Europe PMC (PubMed Central) · Cited by 15 · see citing works
AMPK expression patterns are significantly associated with poor prognosis in breast cancer patients
Al-Maghrabi, J. A., Al‐Sakkaf, K., Qureshi, I. A., Butt, N. S., Damnhory, L., Elshal, M. F., Al-Maghrabi, B., Aldahlawi, A., Ashoor, S., BROWN, B. L., et al. (2017) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2017.05.012 · Cited by 14 · see citing works
Responses to oral glucose challenge differ by physical activity volume and intensity: A pilot study
Simper, T. N., Morris, C., Lynn, A., O’Hagan, C., & Kilner, K. (2017) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2017.04.010 · Cited by 13 · see citing works
Interactions between oxygen homeostasis, food availability, and hydrogen sulfide signaling
Iranon, N. N., & Miller, D. L. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00257 · Cited by 13 · see citing works
Song, G. Y., Kim, S. M., Back, S. H., Yang, S.-B., & Yang, Y. M. (2024) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2024.083 · Cited by 11 · see citing works
Bakker, L. E. H., Guigas, B., van Schinkel, L. D., van der Zon, G. C. M., Streefland, T. C. M., van Klinken, J. B., Jonker, J. T., Lamb, H. J., Smit, J. W. A., Pijl, H., et al. (2014) · Diabetologia · doi:10.1007/s00125-014-3408-4 · Cited by 11 · see citing works
Thabah, D., Syiem, D., Pakyntein, C. L., Banerjee, S., Kharshiing, C. E., & Bhattacharjee, A. (2021) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2021.1897145 · Cited by 11 · see citing works
Lee, M. J.-C., Caruana, N. J., Saner, N. J., Kuang, J., Stokes, T., Mcleod, J. C., Oikawa, S. Y., Bishop, D. J., Bartlett, J. D., & Phillips, S. M. (2023) · The FASEB Journal · doi:10.1096/fj.202302024r · Cited by 10 · see citing works
Contraction stimulates muscle glucose uptake independent of atypical PKC
Yu, H., FUJII, N. L., Toyoda, T., An, D., Farese, R. V., Leitges, M., Hirshman, M. F., Mul, J. D., & Goodyear, L. J. (2015) · Physiological Reports · doi:10.14814/phy2.12565 · Cited by 10 · see citing works
Discovery of donor age markers from bloodstain by LC-MS/MS using a metabolic approach
Kim, H., Lee, Y., Lee, S., Kwon, S., Chun, Y. T., Hyun, S. H., Sung, H. J., Lee, J., & Kang, H. (2021) · International Journal of Legal Medicine · doi:10.1007/s00414-021-02640-w · Cited by 10 · see citing works
Fowler, A., Knaus, K. R., Khuu, S., Khalilimeybodi, A., Schenk, S., Ward, S. R., Fry, A. C., Rangamani, P., & McCulloch, A. D. (2024) · Experimental Physiology · doi:10.1113/ep091712 · Cited by 9 · see citing works
Emerging Link between Tsc1 and FNIP Co-Chaperones of Hsp90 and Cancer
Backe, S. J., Sager, R., Meluni, K. A., Woodford, M. R., Bourboulia, D., & Mollapour, M. (2022) · Biomolecules · doi:10.3390/biom12070928 · Cited by 9 · see citing works
Exploring the Muscle Metabolomics in the Mouse Model of Sepsis-Induced Acquired Weakness
Jiang, Y., Wei, Q., Liu, W., Chen, Q., Chen, X., Yuan, Z., Luo, N., Chen, X., & Wang, C. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/6908488 · Cited by 8 · see citing works
Broholm, C., Mathur, N., Hvid, T., Grøndahl, T. S., Frøsig, C., Pedersen, B. K., & Lindegaard, B. (2013) · Physiological Reports · doi:10.1002/phy2.60 · Cited by 8 · see citing works
Martín-Bernabé, A., Tarragó‐Celada, J., Cunin, V., Michelland, S., Cortés, R., Poignant, J., Boyault, C., Rachidi, W., Bourgoin‐Voillard, S., Cascante, M., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073378 · Cited by 8 · see citing works
Irisin Attenuates Muscle Impairment during Bed Rest through Muscle-Adipose Tissue Crosstalk
D’Amuri, A., Sanz, J. M., Lazzer, S., Pišot, R., Šimunič, B., Biolo, G., Zuliani, G., Gasparini, M., Narici, M. V., Grassi, B., et al. (2022) · Biology · doi:10.3390/biology11070999 · Cited by 7 · see citing works
- Authors
- Hardie, D. G.
- Affiliations
- University of Dundee (GB)
- Corresponding author
- Hardie, D. Grahame
- ORCID
- Hardie, D. Grahame
- Venue
- Proceedings of the Nutrition Society
- Publisher
- Cambridge University Press (CUP)
- Published
- 2010-11-11
- Volume
- 70
- Issue
- 1
- Pages
- 92-99
- ISSN
- 0029-6651 (ISSN-L)
- 1475-2719
- OpenAlex
- W2165667722
- Cited by
- 146
- References
- 73
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 5 · 2022: 7 · 2021: 10 · 2020: 4 · 2019: 8 · 2018: 4 · 2017: 10 · 2016: 6 · 2015: 14 · 2014: 15 · 2013: 15 · 2012: 22
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of The Nutrition Society (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Funders
- Pfizer
- AstraZeneca
- University of Dundee
- Merck KGaA
- Wellcome Trust (080982, 081195)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- AMPK, energy sensing, skeletal muscle metabolism, endurance exercise, resistance training, GLUT4 translocation, glucose uptake, fatty acid oxidation, glycogen synthesis, glycogen synthase phosphorylation, mTOR signaling, mitochondrial biogenesis, AMP/ATP ratio, exercise adaptation
- MeSH terms
- Adenosine Monophosphate, Adenosine Triphosphate, Energy Metabolism, Glucose, Glycogen, Humans, Muscle Contraction, Muscle Proteins, Signal Transduction, Exercise, Muscle, Skeletal, Lipid Metabolism, 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
