The Ever-Expanding Myokinome: Discovery Challenges and Therapeutic Implications
Abstract
Exercise reduces the risk of a multitude of disorders, from metabolic disease to cancer, but the molecular mechanisms mediating the protective effects of exercise are not completely understood. The realization that skeletal muscle is an endocrine organ capable of secreting proteins termed 'myokines', which participate in tissue crosstalk, provided a critical link in the exercise-health paradigm. However, the myokine field is still emerging, and several challenges remain in the discovery and validation of myokines. This Review considers these challenges and highlights some recently identified novel myokines with the potential to be therapeutically exploited in the treatment of metabolic disease and cancer.
Integrity signals
Registry
Cites
Statistics
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?
Exercise induces systemic and tissue-specific adaptations that enhance mitochondrial biogenesis, improve insulin sensitivity, modulate inflammatory pathways, and promote favorable remodeling of skeletal muscle and adipose tissue.
“Exercise induces a range of systemic and tissue-specific adaptations that enhance mitochondrial biogenesis, improve insulin sensitivity, modulate inflammatory pathways, and promote the favorable remodeling of skeletal muscle and adipose tissue [4,5,6].”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [5]
Irisin, FGF21, myostatin, apelin, and Metrnl have direct associations with obesity-related metabolic abnormalities and cardiovascular protection.
“irisin, FGF21, myostatin (MSTN), apelin, and Metrnl have been demonstrated to have direct associations with obesity-related metabolic abnormalities and cardiovascular protection [7,9].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [9]
Cites
Tissue-based map of the human proteome
Uhlén, M., Fagerberg, L., Hallström, B. M., Lindskog, C., Oksvold, P., Mardinoglu, A., Sivertsson, Å., Kampf, C., Sjöstedt, E., Asplund, A., et al. (2015) · Science · doi:10.1126/science.1260419 · Cited by 15,286 · see citing works
A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis
Boström, P., Wu, J., Jedrychowski, M. P., Korde, A., Ye, L., Lo, J. C., Rasbach, K. A., Boström, E. A., Choi, J. H., Long, J. Z., et al. (2012) · Nature · doi:10.1038/nature10777 · Cited by 4,810 · see citing works
Anderson, N. L., & Anderson, N. G. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r200007-mcp200 · Cited by 4,414 · see citing works
Nanoparticle therapeutics: an emerging treatment modality for cancer
Davis, M. E., Chen, Z., & Shin, D. M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2614 · Cited by 4,233 · see citing works
Exercise capacity and mortality among men referred for exercise testing
Myers, J., Prakash, M., Froelicher, V., Do, D., Partington, S., & Atwood, J. E. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa011858 · Cited by 4,114 · see citing works
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013 · see citing works
A gene atlas of the mouse and human protein-encoding transcriptomes
Su, A. I., Wiltshire, T., Batalov, S., Lapp, H., Ching, K. A., Block, D., Zhang, J., Soden, R., Hayakawa, M., Kreiman, G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400782101 · Cited by 3,475 · see citing works
Effect of pegylation on pharmaceuticals
Harris, J. M., & Chess, R. B. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1033 · Cited by 3,431 · see citing works
Biodegradable nanoparticles for drug and gene delivery to cells and tissue
Panyam, J., & Labhasetwar, V. D. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00228-4 · Cited by 3,365 · see citing works
The anti-inflammatory effect of exercise
Petersen, A. M. W., & Pedersen, B. K. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00164.2004 · Cited by 3,100 · see citing works
Muscles, exercise and obesity: skeletal muscle as a secretory organ
Pedersen, B. K., & Febbraio, M. A. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.49 · Cited by 2,909 · see citing works
Lack of Exercise Is a Major Cause of Chronic Diseases
Booth, F. W., Roberts, C. K., & Laye, M. J. (2012) · Comprehensive Physiology · doi:10.1002/cphy.c110025 · Cited by 2,575 · see citing works
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
Muscle as an Endocrine Organ: Focus on Muscle-Derived Interleukin-6
Pedersen, B. K., & Febbraio, M. A. (2008) · Physiological Reviews · doi:10.1152/physrev.90100.2007 · Cited by 2,388 · see citing works
FGF-21 as a novel metabolic regulator
Kharitonenkov, A., Shiyanova, T. L., Koester, A., Ford, A. M., Micanovic, R., Galbreath, E. J., Sandusky, G. E., Hammond, L. J., Moyers, J. S., Owens, R. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23606 · Cited by 2,125 · see citing works
FGF21 regulates PGC-1α and browning of white adipose tissues in adaptive thermogenesis
Fisher, F. M., Kleiner, S., Douris, N., Fox, E. C., Mepani, R. J., Verdeguer, F., Wu, J., Kharitonenkov, A., Flier, J. S., Maratos-Flier, E., et al. (2012) · Genes & Development · doi:10.1101/gad.177857.111 · Cited by 1,478 · see citing works
Vesiclepedia: A Compendium for Extracellular Vesicles with Continuous Community Annotation
Kalra, H., Simpson, R. J., Ji, H., Aikawa, E., Altevogt, P., Askenase, P., Bond, V. C., Borràs, F. E., Breakefield, X., Budnik, V., et al. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001450 · Cited by 1,367 · see citing works
Peterson, A. C., Russell, J. D., Bailey, D. J., Westphall, M. S., & Coon, J. J. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.020131 · Cited by 1,288 · see citing works
Defective Hepatic Autophagy in Obesity Promotes ER Stress and Causes Insulin Resistance
Yang, L., Li, P., Fu, S., Calay, E. S., & Hotamisligil, G. S. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.005 · Cited by 1,274 · see citing works
Adipose tissue browning and metabolic health
Bartelt, A., & Heeren, J. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.204 · Cited by 1,177 · see citing works
Integrative Biology of Exercise
Hawley, J. A., Hargreaves, M., Joyner, M. J., & Zierath, J. R. (2014) · Cell · doi:10.1016/j.cell.2014.10.029 · Cited by 1,152 · see citing works
The abc's (and xyz's) of peptide sequencing
Steen, H., & Mann, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1468 · Cited by 1,139 · see citing works
Steensberg, A., van Hall, G., Osada, T., Sacchetti, M., Saltin, B., & Pedersen, B. K. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00237.x · Cited by 1,095 · see citing works
Fibroblast Growth Factor 21 Corrects Obesity in Mice
Coskun, T., Bina, H. A., Schneider, M. A., Dunbar, J. D., Hu, C. C., Chen, Y., Moller, D. E., & Kharitonenkov, A. (2008) · Endocrinology · doi:10.1210/en.2008-0816 · Cited by 1,031 · see citing works
Rao, R. R., Long, J. Z., White, J. P., Svensson, K. J., Lou, J., Lokurkar, I., Jedrychowski, M. P., Ruas, J. L., Wrann, C. D., Lo, J. C., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.065 · Cited by 973 · see citing works
Ellingsgaard, H., Hauselmann, I., Schuler, B., Habib, A. M., Baggio, L. L., Meier, D. T., Eppler, E., Bouzakri, K., Wueest, S., Muller, Y. D., et al. (2011) · Nature Medicine · doi:10.1038/nm.2513 · Cited by 922 · 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
Pedersen, L., Idorn, M., Olofsson, G. H., Lauenborg, B., Nookaew, I., Hansen, R. H., Johannesen, H. H., Becker, J. C., Pedersen, K. S., Dethlefsen, C., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.01.011 · Cited by 888 · see citing works
Muscle‐derived interleukin‐6: mechanisms for activation and possible biological roles
FEBBRAIO, M. A., & PEDERSEN, B. K. (2002) · The FASEB Journal · doi:10.1096/fj.01-0876rev · Cited by 875 · see citing works
Irisin and FGF21 are cold-induced endocrine activators of brown fat function in humans
Lee, P., Linderman, J. D., Smith, S., Brychta, R. J., Wang, J., Idelson, C., Perron, R. M., Werner, C. D., Phan, G. Q., Kammula, U. S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.017 · Cited by 802 · see citing works
Exercise and IL‐6 infusion inhibit endotoxin‐induced TNF‐α production in humans
Starkie, R., Ostrowski, S. R., Jauffred, S., Febbraio, M., & Pedersen, B. K. (2003) · The FASEB Journal · doi:10.1096/fj.02-0670fje · Cited by 790 · see citing works
Omenn, G. S., States, D. J., Adamski, M., Blackwell, T. W., Menon, R., Hermjakob, H., Apweiler, R., Haab, B. B., Simpson, R. J., Eddes, J. S., et al. (2005) · PROTEOMICS · doi:10.1002/pmic.200500358 · Cited by 787 · see citing works
Interleukin-6 stimulates lipolysis and fat oxidation in humans
van Hall, G., Steensberg, A., Sacchetti, M., Fischer, C., Keller, C., Schjerling, P., Hiscock, N., Møller, K., Saltin, B., Febbraio, M. A., et al. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-021687 · Cited by 767 · see citing works
Barbatelli, G., Murano, I., Madsen, L., Hao, Q., Jimenez, M., Kristiansen, K., Giacobino, J., Matteis, R. D., & Cinti, S. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00600.2009 · Cited by 751 · see citing works
Evidence that interleukin-6 is produced in human skeletal muscle during prolonged running
Ostrowski, K., Rohde, T., Zacho, M., Asp, S., & Pedersen, B. K. (1998) · The Journal of Physiology · doi:10.1111/j.1469-7793.1998.949bp.x · Cited by 673 · see citing works
Cousin, B., Cinti, S., Morroni, M., Raimbault, S., Ricquier, D., Pénicaud, L., & Casteilla, L. (1992) · Journal of Cell Science · doi:10.1242/jcs.103.4.931 · Cited by 665 · see citing works
Roberts, L. D., Boström, P., O’Sullivan, J. F., Schinzel, R. T., Lewis, G. D., Dejam, A., Lee, Y.-K., Palma, M. J., Calhoun, S., Georgiadi, A., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.003 · Cited by 643 · see citing works
Running-induced systemic cathepsin B secretion is associated with memory function
Moon, H. Y., Becke, A., Berron, D., Becker, B., Sah, N., Benoni, G., Janke, E., Lubejko, S. T., Greig, N. H., Mattison, J. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.025 · Cited by 628 · see citing works
Thermogenic Activation Induces FGF21 Expression and Release in Brown Adipose Tissue
Hondares, E., Iglesias, R., Giralt, A., Gonzalez, F. J., Giralt, M., Mampel, T., & Villarroya, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.215889 · Cited by 623 · see citing works
Circulating FGF21 Is Liver Derived and Enhances Glucose Uptake During Refeeding and Overfeeding
Markan, K. R., Naber, M. C., Ameka, M. K., Anderegg, M. D., Mangelsdorf, D. J., Kliewer, S. A., Mohammadi, M., & Potthoff, M. J. (2014) · Diabetes · doi:10.2337/db14-0595 · Cited by 590 · see citing works
Detection and Quantitation of Circulating Human Irisin by Tandem Mass Spectrometry
Jedrychowski, M. P., Wrann, C. D., Paulo, J. A., Gerber, K. K., Szpyt, J., Robinson, M. M., Nair, K. S., Gygi, S. P., & Spiegelman, B. M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.08.001 · Cited by 568 · see citing works
A dual AAV system enables the Cas9-mediated correction of a metabolic liver disease in newborn mice
Yang, Y., Wang, L., Bell, P., McMenamin, D., He, Z., White, J., Yu, H., Xu, C., Morizono, H., Musunuru, K., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3469 · Cited by 556 · see citing works
Exosome-dependent Trafficking of HSP70
Lancaster, G. I., & Febbraio, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502017200 · Cited by 547 · see citing works
Delivery of Therapeutic Proteins
Pisal, D. S., Kosloski, M. P., & Balu-Iyer, S. V. (2010) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22054 · Cited by 532 · see citing works
IL-4 Acts as a Myoblast Recruitment Factor during Mammalian Muscle Growth
Horsley, V., Jansen, K. M., Mills, S. T., & Pavlath, G. K. (2003) · Cell · doi:10.1016/s0092-8674(03)00319-2 · Cited by 508 · see citing works
Suppression of body fat accumulation in myostatin-deficient mice
McPherron, A. C., & Lee, S.-J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213562 · Cited by 505 · see citing works
Exercise as an anti-inflammatory therapy for rheumatic diseases—Myokine regulation
Benatti, F. B., & Pedersen, B. K. (2015) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2014.193 · Cited by 474 · see citing works
Interleukin-6 Is a Novel Factor Mediating Glucose Homeostasis During Skeletal Muscle Contraction
Febbraio, M. A., Hiscock, N., Sacchetti, M., Fischer, C. P., & Pedersen, B. K. (2004) · Diabetes · doi:10.2337/diabetes.53.7.1643 · Cited by 455 · see citing works
Steensberg, A., Febbraio, M. A., Osada, T., Schjerling, P., van Hall, G., Saltin, B., & Pedersen, B. K. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.00633.x · Cited by 444 · see citing works
Therapeutic potential of the endocrine fibroblast growth factors FGF19, FGF21 and FGF23
Degirolamo, C., Sabbà, C., & Moschetta, A. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.9 · Cited by 424 · see citing works
Skeletal muscle as an endocrine organ: PGC-1α, myokines and exercise
Schnyder, S., & Handschin, C. (2015) · Bone · doi:10.1016/j.bone.2015.02.008 · Cited by 419 · see citing works
FGF21 is an Akt‐regulated myokine
Izumiya, Y., Bina, H. A., Ouchi, N., Akasaki, Y., Kharitonenkov, A., & Walsh, K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.10.021 · Cited by 415 · see citing works
Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic lipid homeostasis
Seldin, M. M., Peterson, J. M., Byerly, M. S., Wei, Z., & Wong, G. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336834 · Cited by 406 · see citing works
ALS CNTF Treatment Study Group (1996) · Neurology · doi:10.1212/wnl.46.5.1244 · Cited by 405 · see citing works
Fast/Glycolytic Muscle Fiber Growth Reduces Fat Mass and Improves Metabolic Parameters in Obese Mice
Izumiya, Y., Hopkins, T., Morris, C., Sato, K., Zeng, L., Viereck, J., Hamilton, J. A., Ouchi, N., LeBrasseur, N. K., & Walsh, K. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.003 · Cited by 395 · see citing works
Revisiting the matricellular concept
Murphy-Ullrich, J. E., & Sage, E. H. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.07.005 · Cited by 393 · see citing works
Cancer, Physical Activity, and Exercise
Brown, J. C., Winters‐Stone, K. M., Lee, A. C., & Schmitz, K. H. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120005 · Cited by 379 · see citing works
Nieman, D. C., Davis, J. M., Henson, D. A., Walberg-Rankin, J., Shute, M., Dumke, C. L., Utter, A. C., Vinci, D. M., Carson, J. A., Brown, A., et al. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01130.2002 · Cited by 353 · see citing works
Aoi, W., Naito, Y., Takagi, T., Tanimura, Y., Takanami, Y., Kawai, Y., Sakuma, K., Hang, L. P., Mizushima, K., Hirai, Y., et al. (2013) · Gut · doi:10.1136/gutjnl-2011-300776 · Cited by 347 · see citing works
Irisin – a myth rather than an exercise-inducible myokine
Albrecht, E., Norheim, F., Thiede, B., Holen, T., Ohashi, T., Schering, L., Lee-Ødegård, S., Brenmoehl, J., Thomas, S., Drevon, C. A., et al. (2015) · Scientific Reports · doi:10.1038/srep08889 · Cited by 346 · see citing works
Ouchi, N., Oshima, Y., Ohashi, K., Higuchi, A., Ikegami, C., Izumiya, Y., & Walsh, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803440200 · Cited by 338 · see citing works
Increased secretion and expression of myostatin in skeletal muscle from extremely obese women
Hittel, D. S., Berggren, J. R., Shearer, J., Boyle, K., & Houmard, J. A. (2009) · Diabetes · doi:10.2337/db08-0943 · Cited by 324 · see citing works
States, D. J., Omenn, G. S., Blackwell, T. W., Fermin, D., Eng, J. K., Speicher, D. W., & Hanash, S. (2006) · Nature Biotechnology · doi:10.1038/nbt1183 · Cited by 318 · see citing works
Evidence against a Beneficial Effect of Irisin in Humans
Raschke, S., Elsen, M., Gassenhuber, J., Sommerfeld, M. R., Schwahn, U., Brockmann, B., Jung, R., Wisløff, U., Tjønna, A. E., Raastad, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073680 · Cited by 318 · see citing works
Neill, T., Schaefer, L., & Iozzo, R. V. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.04.029 · Cited by 304 · see citing works
Dynamics of the skeletal muscle secretome during myoblast differentiation
Henningsen, J., Rigbolt, K. T. G., Blagoev, B., Pedersen, B. K., & Kratchmarova, I. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.002113 · Cited by 303 · see citing works
Acute Exercise Induces FGF21 Expression in Mice and in Healthy Humans
Kim, K. H., Kim, S. H., Min, Y.-K., Yang, H.-M., Lee, J.-B., & Lee, M.-S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063517 · Cited by 290 · see citing works
AMPK activity is diminished in tissues of IL-6 knockout mice: the effect of exercise.
Kelly, M., Keller, C., Avilucea, P. R., Keller, P., Luo, Z., Xiang, X., Giralt, M., Hidalgo, J., Saha, A. K., Pedersen, B. K., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.188 · Cited by 289 · see citing works
Systems proteomics of liver mitochondria function
Williams, E. G., Wu, Y., Jha, P., Dubuis, S., Blattmann, P., Argmann, C. A., Houten, S. M., Amariuta, T., Wolski, W., Zamboni, N., et al. (2016) · Science · doi:10.1126/science.aad0189 · Cited by 289 · see citing works
Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics
Räth, T., Baker, K., Dumont, J. A., Peters, R., Jiang, H., Qiao, S., Lencer, W. I., Pierce, G. F., & Blumberg, R. S. (2013) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2013.834293 · Cited by 282 · see citing works
Deshmukh, A. S., Murgia, M., Nagaraj, N., Treebak, J. T., Cox, J., & Mann, M. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.044222 · Cited by 275 · see citing works
Hiscock, N. J., Chan, S. M. H., Bisucci, T., Darby, I. A., & Febbraio, M. A. (2004) · The FASEB Journal · doi:10.1096/fj.03-1259fje · Cited by 273 · see citing works
Exercise-induced muscle-derived cytokines inhibit mammary cancer cell growth
Hojman, P., Dethlefsen, C., Brandt, C., Hansen, J., Pedersen, L., & Pedersen, B. K. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00520.2010 · Cited by 259 · see citing works
From cytokine to myokine: The emerging role of interleukin-6 in metabolic regulation
Pal, M., Febbraio, M. A., & Whitham, M. (2014) · Immunology & Cell Biology · doi:10.1038/icb.2014.16 · Cited by 258 · see citing works
Signaling Specificity of Interleukin-6 Action on Glucose and Lipid Metabolism in Skeletal Muscle
Al-Khalili, L., Bouzakri, K., Glund, S., Lönnqvist, F., Koistinen, H. A., & Krook, A. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0490 · Cited by 250 · see citing works
The Structure of Irisin Reveals a Novel Intersubunit β-Sheet Fibronectin Type III (FNIII) Dimer
Schumacher, M. A., Chinnam, N. B., Ohashi, T., Shah, R., & Erickson, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516641 · Cited by 240 · see citing works
IL-7 is expressed and secreted by human skeletal muscle cells
Haugen, F., Norheim, F., Lian, H., Wensaas, A. J., Dueland, S., Berg, O., Funderud, A., Skålhegg, B. S., Raastad, T., & Drevon, C. A. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00094.2009 · Cited by 237 · see citing works
Initial Quantitative Proteomic Map of 28 Mouse Tissues Using the SILAC Mouse
Geiger, T., Velic, A., Macek, B., Lundberg, E., Kampf, C., Nagaraj, N., Uhlen, M., Cox, J., & Mann, M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.024919 · Cited by 235 · see citing works
Irisin and FNDC5 in retrospect
Erickson, H. (2013) · Adipocyte · doi:10.4161/adip.26082 · Cited by 211 · see citing works
The myokine decorin is regulated by contraction and involved in muscle hypertrophy
Kanzleiter, T., Rath, M., Görgens, S. W., Jensen, J., Tangen, D. S., Kolnes, A. J., Kolnes, K. J., Lee, S., Eckel, J., Schürmann, A., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.06.123 · Cited by 209 · see citing works
Ettinger, M. P., Littlejohn, T. W., Schwartz, S. L., Weiss, S. R., McIlwain, H. H., Heymsfield, S. B., Bray, G. A., Roberts, W. G., Heyman, E. R., Stambler, N., et al. (2003) · PubMed · doi:10.1001/jama.289.14.1826 · Cited by 206 · see citing works
Pharmacologic Effects of FGF21 Are Independent of the “Browning” of White Adipose Tissue
Véniant, M. M., Sivits, G., Helmering, J., Komorowski, R., Lee, J., Fan, W., Moyer, C., & Lloyd, D. J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.019 · Cited by 204 · see citing works
Enhanced growth of tumors in SPARC null mice is associated with changes in the ECM
Brekken, R. A., Puolakkainen, P. A., Graves, D. C., Workman, G. A., Lubkin, S. R., & Sage, E. H. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16804 · Cited by 200 · see citing works
Raschke, S., Eckardt, K., Bjørklund Holven, K., Jensen, J., & Eckel, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062008 · Cited by 199 · see citing works
Musclin is an activity-stimulated myokine that enhances physical endurance
Subbotina, E., Sierra, A., Zhu, Z., Gao, Z., Koganti, S. R. K., Reyes, S., Stepniak, E., Walsh, S. A., Acevedo, M. R., Perez-Terzic, C. M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514250112 · Cited by 198 · see citing works
Starkie, R. L., Arkinstall, M. J., Koukoulas, I., Hawley, J. A., & Febbraio, M. A. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.0585a.x · Cited by 197 · see citing works
Self-citationJe, Y., Jeon, J. Y., Giovannucci, E. L., & Meyerhardt, J. A. (2013) · International Journal of Cancer · doi:10.1002/ijc.28208 · Cited by 194 · see citing works
Low brown adipose tissue activity in endurance-trained compared with lean sedentary men
Vosselman, M. J., Hoeks, J., Brans, B., Pallubinsky, H., Nascimento, E. B. M., van der Lans, A. A. J. J., Broeders, E. P. M., Mottaghy, F. M., Schrauwen, P., & van Marken Lichtenbelt, W. D. (2015) · International Journal of Obesity · doi:10.1038/ijo.2015.130 · Cited by 193 · see citing works
Parabiosis in Mice: A Detailed Protocol
Kamran, P., Sereti, K., Zhao, P., Ali, S. R., Weissman, I. L., & Ardehali, R. (2013) · Journal of Visualized Experiments · doi:10.3791/50556 · Cited by 189 · see citing works
Mapping the human plasma proteome by SCX-LC-IMS-MS
Liu, X., Valentine, S. J., Plasencia, M. D., Trimpin, S., Naylor, S., & Clemmer, D. E. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.04.012 · Cited by 187 · see citing works
Camporez, J.-P. G., Petersen, M. C., Abudukadier, A., Moreira, G. V., Jurczak, M. J., Friedman, G., Haqq, C. M., Petersen, K. F., & Shulman, G. I. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525795113 · Cited by 184 · see citing works
Musclin, a novel skeletal muscle-derived secretory factor
Nishizawa, H., Matsuda, M., Yamada, Y., Kawai, K., Suzuki, E., Makishima, M., Kitamura, T., & Shimomura, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400066200 · Cited by 182 · see citing works
Role of muscle-derived growth factors in bone formation.
Hamrick, M. W., McNeil, P. L., & Patterson, S. L. (2010) · PubMed · Cited by 181 · see citing works
Norheim, F., Raastad, T., Thiede, B., Rustan, A. C., Drevon, C. A., & Haugen, F. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00326.2011 · Cited by 180 · see citing works
Identification of human exercise-induced myokines using secretome analysis
Catoire, M., Mensink, M., Kalkhoven, E., Schrauwen, P., & Kersten, S. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00174.2013 · Cited by 179 · see citing works
Forterre, A. V., Jalabert, A., Berger, E., Baudet, M., Chikh, K., Errazuriz-Cerda, E., Larichaudy, J. D., Chanon, S., Weiss‐Gayet, M., Hesse, A.-M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084153 · Cited by 176 · see citing works
Cell-Type-Resolved Quantitative Proteomics of Murine Liver
Azimifar, S. B., Nagaraj, N., Cox, J., & Mann, M. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.002 · Cited by 173 · see citing works
Secretome profiling of primary human skeletal muscle cells
Hartwig, S., Raschke, S., Knebel, B., Scheler, M., Irmler, M., Paßlack, W., Müller, S., Hanisch, F., Franz, T., Li, X., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.08.004 · Cited by 168 · see citing works
Exercise and regulation of adipokine and myokine production
(2015) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2015.07.002 · Cited by 168 · see citing works
Receptor-Fc fusion therapeutics, traps, and MIMETIBODY™ technology
Huang, C. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.10.010 · Cited by 167 · see citing works
Wilkes, J. J., Lloyd, D. J., & Gekakis, N. (2009) · Diabetes · doi:10.2337/db08-0245 · Cited by 156 · see citing works
Discrete Aspects of FGF21 In Vivo Pharmacology Do Not Require UCP1
Samms, R. J., Smith, D. P., Cheng, C. C., Antonellis, P. P., Perfield, J. W., Kharitonenkov, A., Gimeno, R. E., & Adams, A. C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.046 · Cited by 154 · see citing works
European Code against Cancer 4th Edition: Physical activity and cancer
Leitzmann, M. F., Powers, H. J., Anderson, A. S., Scoccianti, C., Berrino, F., Boutron‐Ruault, M., Cecchini, M., Espina, C., Key, T. J., Norat, T., et al. (2015) · Cancer Epidemiology · doi:10.1016/j.canep.2015.03.009 · Cited by 153 · see citing works
Mass spectrometry of extracellular vesicles
Pòcsfalvi, G., Stanly, C., Vilasi, A., Fiume, I., Capasso, G., Turiák, L., Buzás, E. I., & Vékey, K. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21457 · Cited by 152 · see citing works
Shirazi, R. H., Pálsdóttir, V., Collander, J., Anesten, F., Vogel, H., Langlet, F., Jaschke, A., Schürmann, A., Prévot, V., Shao, R., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306799110 · Cited by 135 · see citing works
Walhin, J., Richardson, J. D., Betts, J. A., & Thompson, D. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.262709 · Cited by 129 · see citing works
gp130 receptor ligands as potential therapeutic targets for obesity
Febbraio, M. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30453 · Cited by 124 · see citing works
Glucagon-to-insulin ratio is pivotal for splanchnic regulation of FGF-21 in humans
Hansen, J. S., Clemmesen, J. O., Secher, N. H., Hoene, M., Drescher, A., Weigert, C., Pedersen, B. K., & Plomgaard, P. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.06.001 · Cited by 123 · see citing works
Seldin, M. M., Lei, X., Tan, S. Y., Stanson, K. P., Wei, Z., & Wong, G. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500736 · Cited by 120 · see citing works
Whitham, M., Chan, M. H. S., Pal, M., Matthews, V. B., Prelovsek, O., Lunke, S., El-Osta, A., Broenneke, H., Alber, J., Brüning, J. C., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310581 · Cited by 107 · see citing works
Regulation of Glucose Fluxes During Exercise in the Postabsorptive State
Wasserman, D. H. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.001203 · Cited by 106 · see citing works
Humoral Nature of the Hypoglycemic Factor of Muscular Work
Goldstein, M. S. (1961) · Diabetes · doi:10.2337/diab.10.3.232 · Cited by 106 · see citing works
Targeting NK Cells for Anticancer Immunotherapy: Clinical and Preclinical Approaches
Carotta, S. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00152 · Cited by 103 · see citing works
Jazayeri, J. A., & Carroll, G. J. (2008) · BioDrugs · doi:10.2165/00063030-200822010-00002 · Cited by 100 · see citing works
Exercise and the Regulation of Adipose Tissue Metabolism
Tsiloulis, T., & Watt, M. J. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.06.016 · Cited by 94 · see citing works
Affinity prefractionation for MS‐based plasma proteomics
Pernemalm, M., Lewensohn, R., & Lehtiö, J. (2009) · PROTEOMICS · doi:10.1002/pmic.200800377 · Cited by 91 · see citing works
Comparative proteomic analysis of the insulin‐induced L6 myotube secretome
Yoon, J. H., Yea, K., Kim, J., Choi, Y. S., Park, S., Lee, H., Lee, C. S., Suh, P., & Ryu, S. H. (2008) · PROTEOMICS · doi:10.1002/pmic.200800187 · Cited by 89 · see citing works
Hepatosplanchnic clearance of interleukin-6 in humans during exercise
Febbraio, M. A., Ott, P., Nielsen, H. B., Steensberg, A., Keller, C., Krustrup, P., Secher, N. H., & Pedersen, B. K. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00134.2003 · Cited by 86 · see citing works
Popielarski, S. R., Hu‐Lieskovan, S., French, S. W., Triche, T. J., & Davis, M. E. (2005) · Bioconjugate Chemistry · doi:10.1021/bc0501146 · Cited by 84 · see citing works
Soria‐Valles, C., Gutiérrez‐Fernández, A., Guiu, M., Mari, B. P., Fueyo, A., Gomis, R. R., & López-Otı́n, C. (2013) · Oncogene · doi:10.1038/onc.2013.267 · Cited by 80 · see citing works
MRM for the verification of cancer biomarker proteins: recent applications to human plasma and serum
Chambers, A. G., Percy, A. J., Simon, R., & Borchers, C. H. (2014) · Expert Review of Proteomics · doi:10.1586/14789450.2014.877346 · Cited by 77 · see citing works
Laye, M. J., Rector, R. S., Borengasser, S. J., Naples, S. P., Uptergrove, G. M., Ibdah, J. A., Booth, F. W., & Thyfault, J. P. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91186.2008 · Cited by 77 · see citing works
Morikawa, T., Kuchiba, A., Lochhead, P. J., Nishihara, R., Yamauchi, M., Imamura, Y., Liao, X., Qian, Z. R., Ng, K., Chan, A. T., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2276 · Cited by 69 · see citing works
Decorin Suppresses Bone Metastasis in a Breast Cancer Cell Line
Araki, K., Wakabayashi, H., Shintani, K., Morikawa, J., Matsumine, A., Kusuzaki, K., Sudo, A., & Uchida, A. (2009) · Oncology · doi:10.1159/000228253 · Cited by 67 · see citing works
Goh, J., Tsai, J. M., Bammler, T. K., Farin, F. M., Endicott, E., & Ladiges, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080123 · Cited by 67 · see citing works
CRISPR–Cas9-mediated genome editing and guide RNA design
Wiles, M. V., Qin, W., Cheng, A. W., & Wang, H. (2015) · Mammalian Genome · doi:10.1007/s00335-015-9565-z · Cited by 66 · see citing works
Expression profiles of active genes in human and mouse livers
Kawamoto, S., Matsumoto, Y., Mizuno, K., Okubo, K., & Matsubara, K. (1996) · Gene · doi:10.1016/0378-1119(96)00512-4 · Cited by 62 · see citing works
Rahman, M., Chan, A. P. K., & Tai, I. T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026390 · Cited by 59 · see citing works
Nicotine induces uncoupling protein 1 in white adipose tissue of obese mice
Yoshida, T., Sakane, N., UMEKAWA, T., Kogure, A., Kondo, M., Kumamoto, K., Kawada, T., Nagase, I., & Saito, M. (1999) · International Journal of Obesity · doi:10.1038/sj.ijo.0800870 · Cited by 58 · see citing works
Introduction to Mass Spectrometry-Based Proteomics
Matthiesen, R., & Bunkenborg, J. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-392-3_1 · Cited by 54 · see citing works
Quantitative analysis of the secretion of the MCP family of chemokines by muscle cells
Henningsen, J., Pedersen, B. K., & Kratchmarova, I. (2010) · Molecular BioSystems · doi:10.1039/c0mb00209g · Cited by 51 · see citing works
Biopharmaceutical Production Technology
(2012) · Wiley eBooks · doi:10.1002/9783527653096 · Cited by 51 · see citing works
Harel, M., Oren‐Giladi, P., Kaidar‐Person, O., Shaked, Y., & Geiger, T. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.043364 · Cited by 49 · see citing works
Yoon, J. H., Kim, D., Jang, J.-H., Ghim, J., Park, S., Song, P., Kwon, Y., Kim, J. J., Hwang, D., Bae, Y., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.039651 · Cited by 46 · see citing works
Korpelainen, R., Lämsä, J., Kaikkonen, K., Korpelainen, J. T., Laukkanen, J. A., Palatsi, I., Takala, T., Ikäheimo, T. M., & Hautala, A. J. (2016) · Annals of Medicine · doi:10.1080/07853890.2016.1178856 · Cited by 44 · see citing works
Hagobian, T. A., & Braun, B. (2006) · Metabolism · doi:10.1016/j.metabol.2005.09.017 · Cited by 40 · see citing works
Targeting gp130 to prevent inflammation and promote insulin action
Kraakman, M. J., Allen, T. L., Whitham, M., Iliades, P., Kammoun, H. L., Estévez, E., Lancaster, G. I., & Febbraio, M. A. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12170 · Cited by 33 · see citing works
Ciliary Neurotrophic Factor: a Role in Obesity?
Duff, E., & Baile, C. A. (2003) · Nutrition Reviews · doi:10.1301/nr.2003.dec.423-426 · Cited by 23 · see citing works
Diabetes, Insulin and Exercise
Richter, E. A., & Galbo, H. (1986) · Sports Medicine · doi:10.2165/00007256-198603040-00004 · Cited by 18 · see citing works
Secretome Analysis of Skeletal Myogenesis Using SILAC and Shotgun Proteomics
Chan, C. Y. X., McDermott, J. C., & Siu, K. W. M. (2011) · International Journal of Proteomics · doi:10.1155/2011/329467 · Cited by 15 · see citing works
Biopharmaceutical production technology
Subramanian, G. (2012) · Cited by 13 · see citing works
Flagged first, then by citations
1 of the 142 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Muscle–Organ Crosstalk: The Emerging Roles of Myokines
Severinsen, M. C. K., & Pedersen, B. K. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa016 · Cited by 1,226 · see citing works
“The role of myokines has previously been reviewed (7, 11-37), identifying more than 650 myokines (38).”
BackgroundExtracellular Vesicles Provide a Means for Tissue Crosstalk during Exercise
Whitham, M., Parker, B. L., Friedrichsen, M. H., Hingst, J. R., Hjorth, M., Hughes, W. E., Egan, C. L., Cron, L., Watt, K. I., Kuchel, R. P., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.001 · Cited by 689 · see citing works
Anti-inflammatory effects of exercise: role in diabetes and cardiovascular disease
Pedersen, B. K. (2017) · European Journal of Clinical Investigation · doi:10.1111/eci.12781 · Cited by 617 · see citing works
Molecular mechanisms linking exercise to cancer prevention and treatment
Hojman, P., Gehl, J., Christensen, J. F., & Pedersen, B. K. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.09.015 · Cited by 600 · 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
Targeting innate immune mediators in type 1 and type 2 diabetes
Donath, M. Y., Dinarello, C. A., & Mandrup-Poulsen, T. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0213-9 · Cited by 416 · see citing works
Bao, H., Cao, J., Chen, M., Min, C., Chen, W., Chen, X., Chen, Y., Chen, Y., Chen, Y., Chen, Z., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2305-0 · Cited by 389 · see citing works
FGF21 as Modulator of Metabolism in Health and Disease
Tezze, C., Romanello, V., & Sandri, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00419 · Cited by 313 · see citing works
Gonzalez-Gil, A. M., & Elizondo-Montemayor, L. (2020) · Nutrients · doi:10.3390/nu12061899 · Cited by 278 · see citing works
“Well-studied myokines [38] are summarized in Table 1, where brief overview on their physiologic role, regulation, and changes in levels or activity in response to exercise is provided.”
BackgroundEndocrine Crosstalk Between Skeletal Muscle and the Brain
Delezie, J., & Handschin, C. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00698 · Cited by 270 · see citing works
Beyond Host Defense: Emerging Functions of the Immune System in Regulating Complex Tissue Physiology
Rankin, L. C., & Artis, D. (2018) · Cell · doi:10.1016/j.cell.2018.03.013 · Cited by 271 · see citing works
Exosome biogenesis, secretion and function of exosomal miRNAs in skeletal muscle myogenesis
Yue, B., Yang, H., Wang, J., Ru, W.-X., Wu, J.-Y., Huang, Y.-Z., Lan, X., Lei, C., & Chen, H. (2020) · Cell Proliferation · doi:10.1111/cpr.12857 · Cited by 231 · see citing works
Training-Induced Changes in Mitochondrial Content and Respiratory Function in Human Skeletal Muscle
Granata, C., Jamnick, N. A., & Bishop, D. J. (2018) · Sports Medicine · doi:10.1007/s40279-018-0936-y · Cited by 247 · see citing works
Hu, C., Zhang, X., Song, P. K., Yuan, Y., Kong, C., Wu, H., Xu, S., Ma, Z., & Tang, Q. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101747 · Cited by 243 · see citing works
Fibroblast growth factor 21 controls mitophagy and muscle mass
Oost, L. J., Kustermann, M., Armani, A., Blaauw, B., & Romanello, V. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12409 · Cited by 231 · see citing works
The molecular athlete: exercise physiology from mechanisms to medals
Furrer, R., Hawley, J. A., & Handschin, C. (2023) · Physiological Reviews · doi:10.1152/physrev.00017.2022 · Cited by 232 · see citing works
Exercise adaptations: molecular mechanisms and potential targets for therapeutic benefit
McGee, S. L., & Hargreaves, M. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0377-1 · Cited by 221 · see citing works
Exercise training in cancer control and treatment
Christensen, J. F., Simonsen, C., & Hojman, P. (2018) · Comprehensive physiology · doi:10.1002/cphy.c180016 · Cited by 203 · see citing works
Exercise-Induced Myokines With Therapeutic Potential for Muscle Wasting
Piccirillo, R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00287 · Cited by 190 · see citing works
Hu, C., Zhang, X., Zhang, N., Wei, W., Li, L., Ma, Z., & Tang, Q. (2020) · Clinical and Translational Medicine · doi:10.1002/ctm2.124 · Cited by 187 · see citing works
Senescence in Post-Mitotic Cells: A Driver of Aging?
von Zglinicki, T., Wan, T., & Miwa, S. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8048 · Cited by 170 · see citing works
Sarcopenia and Cognitive Decline in Older Adults: Targeting the Muscle–Brain Axis
Arosio, B., Calvani, R., Ferri, E., Coelho-Junior, H. J., Carandina, A., Campanelli, F., Ghiglieri, V., Marzetti, E., & Picca, A. (2023) · Nutrients · doi:10.3390/nu15081853 · Cited by 165 · see citing works
The physiology of optimizing health with a focus on exercise as medicine
Pedersen, B. K. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114339 · Cited by 163 · see citing works
Roles of myokines in exercise-induced improvement of neuropsychiatric function
Kim, S., Choi, J., Moon, S., Park, D., Kwak, H., & Kang, J. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02253-8 · Cited by 168 · see citing works
Physical Exercise and Myokines: Relationships with Sarcopenia and Cardiovascular Complications
Barbalho, S. M., Flato, U. A. P., Tofano, R. J., Goulart, R. D. A., Guiguer, E. L., Detregiachi, C. R. P., Buchaim, D. V., Araújo, A. C., Buchaim, R. L., Reina, F. T. R., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103607 · Cited by 156 · see citing works
Burtscher, J., Millet, G. P., Place, N., Kayser, B., & Zanou, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126479 · Cited by 159 · see citing works
Metabolic communication during exercise
Murphy, R. M., Watt, M. J., & Febbraio, M. A. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0258-x · Cited by 158 · see citing works
Circadian rhythms and cancers: the intrinsic links and therapeutic potentials
Zhou, L., Zhang, Z., Nice, E. C., Huang, C., Zhang, W., & Tang, Y. C. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01238-y · Cited by 156 · see citing works
Immunological Implications of Physical Inactivity among Older Adults during the COVID-19 Pandemic
Damiot, A., Pinto, A. J., Turner, J. E., & Gualano, B. (2020) · Gerontology · doi:10.1159/000509216 · Cited by 145 · see citing works
The JAK/STAT Pathway in Skeletal Muscle Pathophysiology
Moresi, V., Adamo, S., & Berghella, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00500 · Cited by 141 · see citing works
The role of extracellular vesicles in skeletal muscle and systematic adaptation to exercise
Vechetti, I. J., Valentino, T., Mobley, C. B., & McCarthy, J. J. (2021) · The Journal of Physiology · doi:10.1113/jp278929 · Cited by 141 · see citing works
Mechanisms by Which Skeletal Muscle Myokines Ameliorate Insulin Resistance
Balakrishnan, R., & Thurmond, D. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094636 · Cited by 132 · see citing works
Inflammation in the Pathophysiology and Therapy of Cardiometabolic Disease
Donath, M. Y., Meier, D. T., & Böni‐Schnetzler, M. (2019) · Endocrine Reviews · doi:10.1210/er.2019-00002 · Cited by 126 · see citing works
Exercise-Induced Irisin Decreases Inflammation and Improves NAFLD by Competitive Binding with MD2
Zhu, W., Sahar, N.-E., Javaid, H. M. A., Pak, E. S., Liang, G., Wang, Y., Ha, H., & Huh, J. Y. (2021) · Cells · doi:10.3390/cells10123306 · Cited by 116 · see citing works
Skeletal muscle adiponectin induction in obesity and exercise
Martínez-Huenchullán, S., Tam, C. S., Ban, L. A., Ehrenfeld-Slater, P., McLennan, S. V., & Twigg, S. M. (2019) · Metabolism · doi:10.1016/j.metabol.2019.154008 · Cited by 117 · see citing works
Placental superoxide dismutase 3 mediates benefits of maternal exercise on offspring health
Kusuyama, J., Alves-Wagner, A. B., Conlin, R. H., Makarewicz, N., Albertson, B. G., Prince, N. B., Kobayashi, S., Kozuka, C., Leth‐Møller, M., Bjerre, M., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.03.004 · Cited by 114 · see citing works
Muscle-to-Brain Signaling Via Myokines and Myometabolites
Rai, M., & Demontis, F. (2022) · Brain Plasticity · doi:10.3233/bpl-210133 · Cited by 121 · see citing works
MacInnis, M. J., McGlory, C., Gibala, M. J., & Phillips, S. M. (2017) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2016-0645 · Cited by 116 · see citing works
Immune system and sarcopenia: Presented relationship and future perspective
Zhang, X., Li, H., He, M., Wang, J., Wu, Y., & Li, Y. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111823 · Cited by 112 · see citing works
Myokines in metabolic homeostasis and diabetes
Eckel, J. (2019) · Diabetologia · doi:10.1007/s00125-019-4927-9 · Cited by 107 · see citing works
Muscle-Organ Crosstalk: Focus on Immunometabolism
Bay, M. L., & Pedersen, B. K. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.567881 · Cited by 110 · see citing works
Biological Aspects of Selected Myokines in Skeletal Muscle: Focus on Aging
Mancinelli, R., Checcaglini, F., Coscia, F., Gigliotti, P. V., Fulle, S., & Fanò, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168520 · Cited by 108 · see citing works
Health benefits of exercise — more than meets the eye!
Febbraio, M. A. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.218 · Cited by 106 · see citing works
Wang, W., Li, M., Chen, Z., Xu, L., Chang, M., Wang, K., Deng, C., Gu, Y., Zhou, S., Shen, Y., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114954 · Cited by 107 · see citing works
McGee, S. L., & Hargreaves, M. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.06.002 · Cited by 105 · see citing works
Disrupted prenatal RNA processing and myogenesis in congenital myotonic dystrophyPreprint
Thomas, J. D., Sznajder, Ł. J., Bardhi, O., Aslam, F. N., Anastasiadis, Z. P., Scotti, M. M., Nishino, I., Nakamori, M., Wang, E. T., & Swanson, M. S. (2017) · Genes & Development · doi:10.1101/gad.300590.117 · Cited by 94 · see citing works
Exercise Improves Vascular Function, but does this Translate to the Brain?
Barnes, J. N., & Corkery, A. T. (2018) · Brain Plasticity · doi:10.3233/bpl-180075 · Cited by 96 · see citing works
Effects of exercise on exosome release and cargo in in vivo and ex vivo models: A systematic review
Estébanez, B., Jiménez‐Pavón, D., Huang, C., Cuevas, M. J., & González‐Gallego, J. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30094 · Cited by 93 · see citing works
IL-6 release from muscles during exercise is stimulated by lactate-dependent protease activity
Højman, P., Brolin, C., Nørgaard-Christensen, N., Dethlefsen, C., Lauenborg, B. T., Olsen, C. K., Åbom, M. M., Krag, T. O. B., Gehl, J., & Pedersen, B. K. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00414.2018 · Cited by 89 · see citing works
Treatment of type 2 diabetes with the designer cytokine IC7Fc
Findeisen, M., Allen, T. L., Henstridge, D. C., Kammoun, H., Brandon, A. E., Baggio, L. L., Watt, K. I., Pal, M., Cron, L., Estevez, E., et al. (2019) · Nature · doi:10.1038/s41586-019-1601-9 · Cited by 86 · see citing works
Jo, D., Yoon, G., Kim, O. Y., & Song, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112636 · Cited by 83 · see citing works
Carson, B. P. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00097 · Cited by 83 · see citing works
Porcine models for studying complications and organ crosstalk in diabetes mellitus
Renner, S., Blutke, A., Clauß, S., Deeg, C. A., Kemter, E., Merkus, D., Wanke, R., & Wolf, E. (2020) · Cell and Tissue Research · doi:10.1007/s00441-019-03158-9 · Cited by 88 · see citing works
The Role of the Skeletal Muscle Secretome in Mediating Endurance and Resistance Training Adaptations
Leuchtmann, A. B., Adak, V., Dilbaz, S., & Handschin, C. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.709807 · Cited by 84 · see citing works
Physical Exercise-Induced Myokines in Neurodegenerative Diseases
Lee, B., Shin, M., Park, Y., Won, S.-Y., & Cho, K. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115795 · Cited by 79 · see citing works
Effect of Various Exercise Regimens on Selected Exercise-Induced Cytokines in Healthy People
Domin, R., Dadej, D., Pytka, M., Zybek-Kocik, A., Ruchała, M., & Guzik, P. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18031261 · Cited by 79 · see citing works
Impact of Lipotoxicity on Tissue “Cross Talk” and Metabolic Regulation
Montgomery, M. K., Nardo, W. D., & Watt, M. J. (2019) · Physiology · doi:10.1152/physiol.00037.2018 · Cited by 78 · see citing works
The wonder exerkines—novel insights: a critical state-of-the-art review
Magliulo, L., Bondi, D., Pini, N., Marramiero, L., & Filippo, E. S. D. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04264-5 · Cited by 74 · see citing works
Nachit, M., & Leclercq, I. A. (2019) · Clinical Science · doi:10.1042/cs20180421 · Cited by 72 · see citing works
Lieberman, D. E., Kistner, T. M., Richard, D. J., Lee, I.-M. M., & Baggish, A. L. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2107621118 · Cited by 73 · see citing works
Muscle cell-derived cytokines in skeletal muscle regeneration
Waldemer-Streyer, R., Kim, D., & Chen, J. (2022) · The FEBS Journal · doi:10.1111/febs.16372 · Cited by 64 · see citing works
Ansari, E., Chargi, N., van Gemert, J. T. M., van Es, R. J. J., Dieleman, F. J., Rosenberg, A. J. W. P., Cann, E. M. V., & de Bree, R. (2019) · Oral Oncology · doi:10.1016/j.oraloncology.2019.104530 · Cited by 70 · see citing works
Hawley, J. A., Forster, S. C., & Giles, E. M. (2025) · Gastroenterology · doi:10.1053/j.gastro.2025.01.224 · Cited by 69 · see citing works
Loss of neuromuscular junction integrity and muscle atrophy in skeletal muscle disuse
Sirago, G., Pellegrino, M. A., Bottinelli, R., Franchi, M. V., & Narici, M. V. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101810 · Cited by 66 · see citing works
Exerkines and cardiometabolic benefits of exercise: from bench to clinic
Jin, L., Díaz-Cañestro, C., Wang, Y., Tse, M. A., & Xu, A. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00027-z · Cited by 68 · see citing works
Myokines: a descriptive review
Barbalho, S. M., Neto, E. V. P., Goulart, R. D. Á., Bechara, M. D., Chagas, E. F. B., Audi, M., Campos, L. M. G., Guiguer, É. L., Buchaim, R. L., Buchaim, D. V., et al. (2020) · The Journal of Sports Medicine and Physical Fitness · doi:10.23736/s0022-4707.20.10884-3 · Cited by 67 · see citing works
Re Cecconi, A. D., Forti, M., Chiappa, M., Zhu, Z., Zingman, L. V., Cervo, L., Beltrame, L., Marchini, S., & Piccirillo, R. (2019) · Cancers · doi:10.3390/cancers11101541 · Cited by 66 · see citing works
Chan, W., Chin, S. H., Phillips, A. C., Jones, D. A., Kaur, O., Bosch, J. A., & Borrows, R. (2019) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2019.06.009 · Cited by 64 · see citing works
Fuller, O. K., Whitham, M., Mathivanan, S., & Febbraio, M. A. (2020) · Cells · doi:10.3390/cells9102182 · Cited by 60 · see citing works
Muscoloskeletal aging, sarcopenia and cancer
Colloca, G. A., Capua, B. D., Bellieni, A., Cesari, M., Marzetti, E., Valentini, V., & Calvani, R. (2018) · Journal of Geriatric Oncology · doi:10.1016/j.jgo.2018.11.007 · Cited by 64 · see citing works
Kurgan, N., Tsakiridis, E. E., Kouvelioti, R., Moore, J., Klentrou, P., & Tsiani, E. (2017) · Cancers · doi:10.3390/cancers9050046 · Cited by 58 · see citing works
Babaei, P., & Azari, H. B. (2022) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2021.771553 · Cited by 61 · see citing works
Follistatin-like 1 as a Novel Adipomyokine Related to Insulin Resistance and Physical Activity
Xu, X., Zhang, T., Mokou, M., Li, L., Li, P., Song, J., Liu, H., Zhu, Z., Liu, D., Yang, M., et al. (2020) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaa629 · Cited by 57 · see citing works
Myokines: Metabolic regulation in obesity and type 2 diabetes
Chen, Z.-T., Weng, Z.-X., Lin, J. D., & Meng, Z.-X. (2024) · Life Metabolism · doi:10.1093/lifemeta/loae006 · Cited by 58 · see citing works
Irisin: An anti-inflammatory exerkine in aging and redox-mediated comorbidities
Trettel, C. D. S., Pelozin, B. R. D. A., Barros, M. P., Bachi, A. L. L., Braga, P. G. S., Momesso, C. M., Furtado, G. E., Valente, P. A., de Oliveira, E. M., Hogervorst, E., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1106529 · Cited by 55 · see citing works
Role of exercise-induced hepatokines in metabolic disorders
Ennequin, G., Sirvent, P., & Whitham, M. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00433.2018 · Cited by 54 · see citing works
Impact of Sarcopenia on Outcomes of Autologous Head and Neck Free Tissue Reconstruction
Jones, A. J., Alwani, M. M., Novinger, L. J., Pittelkow, E. M., Bonetto, A., Sim, M. W., Moore, M. G., & Mantravadi, A. V. (2020) · Journal of Reconstructive Microsurgery · doi:10.1055/s-0040-1701696 · Cited by 54 · see citing works
Current advances in our understanding of exercise as medicine in metabolic disease
Sylow, L., & Richter, E. A. (2019) · Current Opinion in Physiology · doi:10.1016/j.cophys.2019.04.008 · Cited by 51 · see citing works
Exercise and the Skeletal Muscle EpigenomePreprint
McGee, S. L., & Walder, K. R. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029876 · Cited by 54 · see citing works
Muscle-secreted neurturin couples myofiber oxidative metabolism and slow motor neuron identity
Correia, J. C., Kelahmetoglu, Y., Jannig, P. R., Schweingruber, C., Shvaikovskaya, D., Zhengye, L., Červenka, I., Khan, N. P., Stec, M. J., Oliveira, M. M. S., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.09.003 · Cited by 50 · see citing works
Raun, S. H., Ali, M. S., Kjøbsted, R., Møller, L. L. V., Federspiel, M. A., Richter, E. A., Jensen, T. E., & Sylow, L. (2018) · The Journal of Physiology · doi:10.1113/jp275602 · Cited by 51 · see citing works
Baranova, A. V., Maltseva, D. V., & Tonevitsky, A. (2018) · Obesity Reviews · doi:10.1111/obr.12765 · Cited by 52 · see citing works
Gut microbiota and regulation of myokine-adipokine function
Suriano, F., Hul, M. V., & Cani, P. D. (2020) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2020.03.006 · Cited by 50 · see citing works
Doncheva, A. I., Romero, S., Ramírez‐Garrastacho, M., Lee-Ødegård, S., Kolnes, K. J., Tangen, D. S., Olsén, T., Drevon, C. A., Llorente, A., Dalen, K. T., et al. (2022) · Acta Physiologica · doi:10.1111/apha.13862 · Cited by 49 · see citing works
Darragh, I. A. J., O’Driscoll, L., & Egan, B. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.738333 · Cited by 48 · see citing works
Proteomic serum biomarkers for neuromuscular diseases
Murphy, S., Zweyer, M., Mundegar, R. R., Swandulla, D., & Ohlendieck, K. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1429923 · Cited by 47 · see citing works
A systematic review and meta-analysis demonstrating Klotho as an emerging exerkine
Corrêa, H. D. L., Raab, A. T. O., Araújo, T. M., Deus, L. A., Reis, A. L., Honorato, F. S., Rodrigues-Silva, P. L., Neves, R. V. P., Brunetta, H. S., Mori, M. A., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-22123-1 · Cited by 44 · see citing works
Sawada, M., Yamamoto, H., Ogasahara, A., Tanaka, Y., & Kihara, S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.06.141 · Cited by 44 · see citing works
Time Course and Role of Exercise-Induced Cytokines in Muscle Damage and Repair After a Marathon Race
Zocoler, C. A. S., Sierra, A., Galán, B. S. M., Maciel, J. F. D. S., Manoel, R., Barbeiro, H. V., de Souza, H. P., & Cury‐Boaventura, M. F. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.752144 · Cited by 43 · see citing works
Myokines and Microbiota: New Perspectives in the Endocrine Muscle–Gut Axis
Saponaro, F., Bertolini, A., Baragatti, R., Galfo, L., Chiellini, G., Saba, A., & D’Urso, G. (2024) · Nutrients · doi:10.3390/nu16234032 · Cited by 43 · see citing works
Clinical Significance of Sarcopenia among Patients with Advanced Oropharyngeal Cancer
Tamaki, A., Manzoor, N. F., Babajanian, E. E., Ascha, M. S., Rezaee, R. P., & Zender, C. A. (2018) · Otolaryngology · doi:10.1177/0194599818793857 · Cited by 43 · see citing works
Aoi, W., Hirano, N., Lassiter, D. G., Björnholm, M., Chibalin, A., Sakuma, K., Tanimura, Y., Mizushima, K., Takagi, T., Naito, Y., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900453r · Cited by 43 · see citing works
Tero-Vescan, A., Degens, H., Matsakas, A., Ștefănescu, R., Ősz, B. E., & Slevin, M. (2025) · Pharmaceuticals · doi:10.3390/ph18081222 · Cited by 44 · see citing works
Myotonic Dystrophy and Developmental Regulation of RNA Processing
Thomas, J. D., Oliveira, R., Sznajder, Ł. J., & Swanson, M. S. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170002 · Cited by 47 · see citing works
Infection and chronic disease activate a systemic brain-muscle signaling axis
Yang, S., Tian, M., Dai, Y., Wang, R., Yamada, S., Feng, S., Wang, Y., Chhangani, D., Ou, T., Li, W., et al. (2024) · Science Immunology · doi:10.1126/sciimmunol.adm7908 · Cited by 58 · see citing works
Personalized physiological medicine
İnce, C. (2017) · Critical Care · doi:10.1186/s13054-017-1907-7 · Cited by 40 · see citing works
Exploring inter-organ crosstalk to uncover mechanisms that regulate β-cell function and mass
Shirakawa, J., Jesus, D. F. D., & Kulkarni, R. (2017) · European Journal of Clinical Nutrition · doi:10.1038/ejcn.2017.13 · Cited by 39 · see citing works
Beta-klotho in type 2 diabetes mellitus: From pathophysiology to therapeutic strategies
Hua, S., Liu, Q., Li, J., Fan, M., Yan, K., & Ye, D. (2021) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-021-09661-1 · Cited by 39 · see citing works
Muscle-Derived Cytokines Reduce Growth, Viability and Migratory Activity of Pancreatic Cancer Cells
Schwappacher, R., Dieterich, W., Reljic, D., Pilarsky, C. P., Mukhopadhyay, D., Chang, D. K.-F., Biankin, A. V., Siebler, J., Herrmann, H. J., Neurath, M. F., et al. (2021) · Cancers · doi:10.3390/cancers13153820 · Cited by 39 · see citing works
The Therapeutic Potential of Anti-Inflammatory Exerkines in the Treatment of Atherosclerosis
Yu, M., Tsai, S., & Kuo, Y. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061260 · Cited by 39 · see citing works
- Authors
- Whitham, M., & Febbraio, M. A.
- Affiliations
- Garvan Institute of Medical Research (AU)
- Corresponding author
- Febbraio, Mark A.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2016-09-12
- Volume
- 15
- Issue
- 10
- Pages
- 719-729
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W2518700063
- Cited by
- 279
- References
- 142
- Citations by year
- 2026: 28 · 2025: 17 · 2024: 25 · 2023: 23 · 2022: 35 · 2021: 36 · 2020: 35 · 2019: 38 · 2018: 29 · 2017: 13
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Drug Discovery (publishedVersion)
- PubMed (publishedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
- Topics
- Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- myokines, physical activity, skeletal muscle endocrine function, cancer therapy, metabolic disease treatment, tissue crosstalk
- MeSH terms
- Animals, Humans, Metabolic Diseases, Muscle Proteins, Neoplasms, Exercise, Interleukin-6, Muscle, Skeletal, Drug Discovery
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