The Role of the Skeletal Muscle Secretome in Mediating Endurance and Resistance Training Adaptations

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

Neurotrophins: Roles in Neuronal Development and Function

Huang, E. J., & Reichardt, L. F. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.677 · Cited by 4,394 · 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

Matrix Metalloproteinases

Nagase, H., & Woessner, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21491 · Cited by 3,905 · see citing works

Exercise as medicine - evidence for prescribing exercise as therapy in 26 different chronic diseases

Pedersen, B. K., & Saltin, B. (2015) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1111/sms.12581 · Cited by 3,514 · see citing works

Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway

HEINRICH, P. C., BEHRMANN, I., MÜLLER-NEWEN, G., SCHAPER, F., & GRAEVE, L. (1998) · Biochemical Journal · doi:10.1042/bj3340297 · Cited by 2,130 · see citing works

Exercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation

Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084 · see citing works

Isolation and Characterization of a Novel Endogenous Peptide Ligand for the Human APJ Receptor

Tatemoto, K., Hosoya, M., Habata, Y., Fujii, R., Kakegawa, T., Zou, M.-X., Kawamata, Y., Fukusumi, S., Hinuma, S., Kitada, C., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9489 · Cited by 1,684 · see citing works

Regulation of myostatin activity and muscle growth

Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616 · see citing works

Role of PFKFB3-Driven Glycolysis in Vessel Sprouting

Bock, K. D., Γεωργιάδου, Μ., Schoors, S., Kuchnio, A., Wong, B. W., Cantelmo, A. R., Quaegebeur, A., Ghesquière, B., Cauwenberghs, S., Eelen, G., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.037 · Cited by 1,559 · see citing works

Cloning of a T Cell Growth Factor that Interacts with the β Chain of the Interleukin-2 Receptor

Grabstein, K. H., Eisenman, J. R., Shanebeck, K. D., Rauch, C. T., Srinivasan, S., Fung, V., Beers, C., Richardson, J. S., Schoenborn, M. A., Ahdieh, M., et al. (1994) · Science · doi:10.1126/science.8178155 · Cited by 1,422 · see citing works

Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child

Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399 · see citing works

IL-8 Directly Enhanced Endothelial Cell Survival, Proliferation, and Matrix Metalloproteinases Production and Regulated Angiogenesis

Li, A., Dubey, S., Varney, M. L., Davé, B. J., & Singh, R. K. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.6.3369 · Cited by 1,324 · see citing works

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 · cited 3× · see citing works

A systematic review, meta-analysis and meta-regression of the effect of protein supplementation on resistance training-induced gains in muscle mass and strength in healthy adults

Morton, R. W., Murphy, K. T., McKellar, S. R., Schoenfeld, B. J., Henselmans, M., Helms, E., Aragon, A. A., Devries, M. C., Banfield, L., Krieger, J. W., et al. (2018) · British Journal of Sports Medicine · doi:10.1136/bjsports-2017-097608 · Cited by 1,154 · see citing works

Production of interleukin-6 in contracting human skeletal muscles can account for the exercise-induced increase in plasma interleukin-6

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

HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1α

Arany, Z., Foo, S.-Y., Ma, Y., Ruas, J. L., Bommi-Reddy, A., Girnun, G., Cooper, M., Laznik, D., Chinsomboon, J., Rangwala, S. M., et al. (2008) · Nature · doi:10.1038/nature06613 · Cited by 1,054 · see citing works

Essential involvement of interleukin-8 (IL-8) in acute inflammation

Harada, A., Sekido, N., Akahoshi, T., Wada, T., Mukaida, N., & Matsushima, K. (1994) · Journal of Leukocyte Biology · doi:10.1002/jlb.56.5.559 · Cited by 1,041 · see citing works

Myostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation

Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014 · see citing works

Meteorin-like is a hormone that regulates immune-adipose interactions to increase beige fat thermogenesis

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

Evidence for a release of brain-derived neurotrophic factor from the brain during exercise

Rasmussen, P., Brassard, P., Adser, H., Pedersen, M. V., Leick, L., Hart, E., Secher, N. H., Pedersen, B. K., & Pilegaard, H. (2009) · Experimental Physiology · doi:10.1113/expphysiol.2009.048512 · Cited by 914 · see citing works

Citric acid cycle intermediates as ligands for orphan G-protein-coupled receptors

He, W., Miao, F. J.-P., Lin, D. C.-H., Schwandner, R. T., Wang, Z., Gao, J., Chen, J.-L., Tian, H., & Ling, L. (2004) · Nature · doi:10.1038/nature02488 · Cited by 909 · see citing works

Interleukin-6 Is an Essential Regulator of Satellite Cell-Mediated Skeletal Muscle Hypertrophy

Serrano, A. L., Baeza-Raja, B., Perdiguero, E., Jardí, M., & Muñoz-Cánoves, P. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.011 · Cited by 873 · cited 6× · see citing works

The effect of acute exercise on serum brain-derived neurotrophic factor levels and cognitive function.

FERRIS, L. T., WILLIAMS, J. S., & SHEN, C.-L. (2007) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31802f04c7 · Cited by 849 · see citing works

Lack of neurotrophin-3 leads to deficiencies in the peripheral nervous system and loss of limb proprioceptive afferents

Ernfors, P., Lee, K., Kučera, J., & Jaenisch, R. (1994) · Cell · doi:10.1016/0092-8674(94)90213-5 · Cited by 805 · 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

Myostatin negatively regulates satellite cell activation and self-renewal

McCroskery, S., Thomas, M., Maxwell, L., Sharma, M., & Kambadur, R. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207056 · Cited by 784 · 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

Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase

Matthews, V. B., Åström, M.-B., Chan, M. H. S., Bruce, C. R., Krabbe, K. S., Prelovsek, O., Åkerström, T., Yfanti, C., Broholm, C., Mortensen, O. H., et al. (2009) · Diabetologia · doi:10.1007/s00125-009-1364-1 · Cited by 722 · see citing works

The Mitochondrial-Derived Peptide MOTS-c Promotes Metabolic Homeostasis and Reduces Obesity and Insulin Resistance

Lee, C., Zeng, J., Drew, B. G., Sallam, T., Martin-Montalvo, A., Wan, J., Kim, S.-J., Mehta, H., Hevener, A. L., de Cabo, R., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.009 · Cited by 715 · see citing works

Anatomical Profiling of G Protein-Coupled Receptor Expression

Regard, J. B., Sato, I. T., & Coughlin, S. R. (2008) · Cell · doi:10.1016/j.cell.2008.08.040 · Cited by 696 · see citing works

Extracellular 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

A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy

Ruas, J. L., White, J. P., Rao, R. R., Kleiner, S., Brannan, K. T., Harrison, B. C., Greene, N. P., Wu, J., Estall, J. L., Irving, B. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.050 · Cited by 677 · see citing works

β-Aminoisobutyric Acid Induces Browning of White Fat and Hepatic β-Oxidation and Is Inversely Correlated with Cardiometabolic Risk Factors

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

Disruption of the neurotrophin-3 receptor gene trkC eliminates la muscle afferents and results in abnormal movements

Klein, R., Silos‐Santiago, I., Smeyne, R. J., Lira, S. A., Brambilla, R., Bryant, S., Zhang, L., Snider, W. D., & Barbacid, M. (1994) · Nature · doi:10.1038/368249a0 · Cited by 623 · 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

IL-6-induced skeletal muscle atrophy

Haddad, F., Zaldivar, F., Cooper, D. M., & Adams, G. R. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01026.2004 · Cited by 612 · see citing works

Adaptations to Endurance and Strength TrainingPreprint

Hughes, D. C., Ellefsen, S., & Baar, K. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029769 · Cited by 583 · see citing works

FOXO1 couples metabolic activity and growth state in the vascular endothelium

Wilhelm, K., Happel, K., Eelen, G., Schoors, S., Oellerich, M. F., Lim, R., Zimmermann, B., Aspalter, I. M., Franco, C. A., Boettger, T., et al. (2016) · Nature · doi:10.1038/nature16498 · Cited by 579 · see citing works

Cardiac natriuretic peptides

Goetze, J. P., Bruneau, B. G., Ramos, H. R., Ogawa, T., de Bold, M. L. K., & de Bold, A. J. (2020) · Nature Reviews Cardiology · doi:10.1038/s41569-020-0381-0 · Cited by 546 · see citing works

Evidence that brain-derived neurotrophic factor is a trophic factor for motor neurons in vivo

Koliatsos, V. E., Clatterbuck, R. E., Winslow, J. W., Cayouette, M. H., & Prices, D. L. (1993) · Neuron · doi:10.1016/0896-6273(93)90326-m · Cited by 539 · see citing works

Accumulation of succinate controls activation of adipose tissue thermogenesis

Mills, E. L., Pierce, K. A., Jedrychowski, M. P., Garrity, R., Winther, S., Vidoni, S., Yoneshiro, T., Spinelli, J. B., Lu, G. Z., Kazak, L., et al. (2018) · Nature · doi:10.1038/s41586-018-0353-2 · Cited by 539 · see citing works

Endothelial Lactate Controls Muscle Regeneration from Ischemia by Inducing M2-like Macrophage Polarization

Zhang, J., Muri, J., Fitzgerald, G., Gorski, T., Giannì-Barrera, R., Masschelein, E., D’Hulst, G., Gilardoni, P. A., Turiel, G., Fan, Z., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.05.004 · Cited by 538 · see citing works

IGF-Binding Proteins: Why Do They Exist and Why Are There So Many?

Allard, J. B., & Duan, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00117 · Cited by 517 · 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

Succinate, an intermediate in metabolism, signal transduction, ROS, hypoxia, and tumorigenesis.

Tretter, L., Patócs, A., & Chinopoulos, C. (2016) · Biochimica et Biophysica Acta · doi:10.1016/j.bbabio.2016.03.012 · Cited by 502 · see citing works

Mitochondrial biogenesis by NO yields functionally active mitochondria in mammals

Nisoli, E., Falcone, S., Tonello, C., Cozzi, V., Palomba, L., Fiorani, M., Pisconti, A., Brunelli, S., Cardile, A., Francolini, M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405432101 · Cited by 495 · see citing works

Identification and functional analysis of endothelial tip cell–enriched genes

del Toro, R., Prahst, C., Mathivet, T., Siegfried, G., Kaminker, J. S., Larrivee, B., Breant, C., Duarte, A., Takakura, N., Fukamizu, A., et al. (2010) · Blood · doi:10.1182/blood-2010-02-270819 · Cited by 474 · see citing works

Strength Training with Blood Flow Restriction Diminishes Myostatin Gene Expression

Laurentino, G. C., Ugrinowitsch, C., Roschel, H., Aoki, M. S., Soares, A. G., Neves, M., Aihara, A. Y., Fernandes, A. D. R. C., & Tricoli, V. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318233b4bc · Cited by 466 · 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

Interleukin‐6 production in contracting human skeletal muscle is influenced by pre‐exercise muscle glycogen content

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

Skeletal Muscle Extracellular Matrix – What Do We Know About Its Composition, Regulation, and Physiological Roles? A Narrative Review

Csapo, R., Gumpenberger, M., & Wessner, B. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00253 · Cited by 432 · see citing works

Lack of myostatin results in excessive muscle growth but impaired force generation

Amthor, H., Macharia, R., Navarrete, R., Schuelke, M., Brown, S., Otto, A., Voït, T., Francesco Muntoni, A., Vrbovà, G., Partridge, T. A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604893104 · Cited by 425 · see citing works

Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice.

Tsujinaka, T., Fujita, J., Ebisui, C., Yano, M., Kominami, E., Suzuki, K., Tanaka, K., Katsume, A., Ohsugi, Y., Shiozaki, H., et al. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118398 · Cited by 421 · 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

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

Neither load nor systemic hormones determine resistance training-mediated hypertrophy or strength gains in resistance-trained young men

Morton, R. W., Oikawa, S. Y., Wavell, C. G., Mazara, N., McGlory, C., Quadrilatero, J., Baechler, B. L., Baker, S. K., & Phillips, S. M. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00154.2016 · Cited by 404 · see citing works

Exercise-Induced Changes in Visceral Adipose Tissue Mass Are Regulated by IL-6 Signaling: A Randomized Controlled Trial

Wedell-Neergaard, A.-S., Lang Lehrskov, L., Christensen, R. H., Legaard, G. E., Dorph, E., Larsen, M. K., Launbo, N., Fagerlind, S. R., Seide, S. K., Nymand, S., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2018.12.007 · Cited by 403 · see citing works

Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis

Amthor, H., Nicholas, G., McKinnell, I., Kemp, C. F., Sharma, M., Kambadur, R., & Patel, K. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.01.046 · Cited by 401 · see citing works

The exerkine apelin reverses age-associated sarcopenia

Vinel, C., Lukjanenko, L., Batut, A., Deleruyelle, S., Pradère, J.-P., Le Gonidec, S., Dortignac, A., Geoffre, N., Pereira, O., Karaz, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0131-6 · Cited by 398 · see citing works

Postexercise hypotension and sustained postexercise vasodilatation: what happens after we exercise?

Halliwill, J. R., Buck, T. M., Lacewell, A. N., & Romero, S. A. (2012) · Experimental Physiology · doi:10.1113/expphysiol.2011.058065 · Cited by 390 · see citing works

High-Dimensional Single-Cell Cartography Reveals Novel Skeletal Muscle-Resident Cell Populations

Giordani, L., He, G. J., Négroni, E., Sakai, H., Law, J., Siu, M. M., Wan, R., Corneau, A., Tajbakhsh, S., Cheung, T. H., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.026 · Cited by 389 · see citing works

Sorting Mechanisms for MicroRNAs into Extracellular Vesicles and Their Associated Diseases

Groot, M., & Lee, H. (2020) · Cells · doi:10.3390/cells9041044 · Cited by 386 · see citing works

The CXC chemokines, IL-8 and IP-10, regulate angiogenic activity in idiopathic pulmonary fibrosis

Keane, M. P., Arenberg, D. A., Lynch, J. P., Whyte, R. I., Iannettoni, M. D., Burdick, M. D., Wilke, C. A., Morris, S. B., Glass, M., DiGiovine, B., et al. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.3.1437 · Cited by 382 · see citing works

Localized infusion of IGF-I results in skeletal muscle hypertrophy in rats

Adams, G. R., & McCue, S. A. (1998) · Journal of Applied Physiology · doi:10.1152/jappl.1998.84.5.1716 · Cited by 377 · see citing works

Myogenic progenitor cells control extracellular matrix production by fibroblasts during skeletal muscle hypertrophy

Fry, C. S., Kirby, T. J., Kosmac, K., McCarthy, J. J., & Peterson, C. A. (2017) · Cell stem cell · doi:10.1016/j.stem.2016.09.010 · Cited by 372 · see citing works

Impact of a Competitive Marathon Race on Systemic Cytokine and Neutrophil Responses

Suzuki, K., Nakaji, S., Yamada, M., Liu, Q., Kurakake, S., Okamura, N., Kumae, T., Umeda, T., & Sugawara, K. (2003) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000048861.57899.04 · Cited by 366 · see citing works

Stimuli and sensors that initiate skeletal muscle hypertrophy following resistance exercise

Wackerhage, H., Schoenfeld, B. J., Hamilton, D. L., Lehti, M., & Hulmi, J. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00685.2018 · Cited by 357 · see citing works

Carbohydrate ingestion influences skeletal muscle cytokine mRNA and plasma cytokine levels after a 3-h run

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

Loading recommendations for muscle strength, hypertrophy, and local endurance: a re-examination of the repetition continuum.

Schoenfeld, B. J., Grgic, J., Van Every, D. W., & Plotkin, D. L. (2021) · Sports · doi:10.3390/sports9020032 · Cited by 334 · see citing works

Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo

Cox, C. M., D'Agostino, S. L., Miller, M. K., Heimark, R. L., & Krieg, P. A. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.04.452 · Cited by 328 · see citing works

SPARC, a matricellular protein: at the crossroads of cell–matrix

Brekken, R. A., & Sage, E. H. (2000) · Matrix Biology · doi:10.1016/s0945-053x(00)00105-0 · Cited by 327 · see citing works

Single-cell transcriptional profiles in human skeletal muscle

Rubenstein, A. B., Smith, G. R., Raue, U., Begue, G., Minchev, K., Ruf-Zamojski, F., Nair, V. D., Wang, X., Zhou, L., Zaslavsky, E., et al. (2020) · Scientific Reports · doi:10.1038/s41598-019-57110-6 · Cited by 323 · see citing works

Monocyte/Macrophage-derived IGF-1 Orchestrates Murine Skeletal Muscle Regeneration and Modulates Autocrine Polarization.

Tonkin, J. N., Temmerman, L., Sampson, R., Gallego-Colon, E., Barberi, L., Bilbao, D., Schneider, M., Musarò, A., & Rosenthal, N. (2015) · Molecular Therapy · doi:10.1038/mt.2015.66 · Cited by 322 · see citing works

Quadrupling Muscle Mass in Mice by Targeting TGF-ß Signaling Pathways

Lee, S.-J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000789 · Cited by 316 · see citing works

Myostatin/activin pathway antagonism: molecular basis and therapeutic potential

Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314 · see citing works

The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress

Kim, K. H., Son, J. M., Benayoun, B. A., & Lee, C. D. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.06.008 · Cited by 311 · see citing works

Molecular Transducers of Physical Activity Consortium (MoTrPAC): Mapping the Dynamic Responses to Exercise

Sanford, J. A., Nogiec, C. D., Lindholm, M. E., Adkins, J., Amar, D., Dasari, S., Drugan, J. K., Fernández, F. M., Radom‐Aizik, S., Schenk, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.004 · Cited by 300 · see citing works

Resistance exercise‐induced increases in putative anabolic hormones do not enhance muscle protein synthesis or intracellular signalling in young men

West, D. W. D., Kujbida, G. W., Moore, D. R., Atherton, P., Burd, N. A., Padzik, J. P., De Lisio, M., Tang, J. E., Parise, G., Rennie, M. J., et al. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.177220 · Cited by 289 · see citing works

Natriuretic Peptides/cGMP/cGMP-Dependent Protein Kinase Cascades Promote Muscle Mitochondrial Biogenesis and Prevent Obesity

Miyashita, K., Itoh, H., Tsujimoto, H., Tamura, N., Fukunaga, Y., Sone, M., Yamahara, K., Taura, D., Inuzuka, M., Sonoyama, T., et al. (2009) · Diabetes · doi:10.2337/db09-0393 · Cited by 288 · see citing works

The relationships among IGF-1, DNA content, and protein accumulation during skeletal muscle hypertrophy

Adams, G. R., & Haddad, F. (1996) · Journal of Applied Physiology · doi:10.1152/jappl.1996.81.6.2509 · Cited by 287 · see citing works

Humanin: a harbinger of mitochondrial-derived peptides

Lee, C., Yen, K., & Cohen, P. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.01.005 · Cited by 284 · see citing works

Effect of high intensity training on capillarization and presence of angiogenic factors in human skeletal muscle

Jensen, L., Bangsbo, J., & Hellsten, Y. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2003.057711 · Cited by 281 · see citing works

The Ever-Expanding Myokinome: Discovery Challenges and Therapeutic Implications

Whitham, M., & Febbraio, M. A. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.153 · Cited by 279 · see citing works

pH-gated succinate secretion regulates muscle remodeling in response to exercise

Reddy, A., Bozi, L. H. M., Yaghi, O. K., Mills, E. L., Xiao, H., Nicholson, H. E., Paschini, M., Paulo, J. A., Garrity, R., Laznik-Bogoslavski, D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.039 · Cited by 279 · see citing works

The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review

Gonzalez-Gil, A. M., & Elizondo-Montemayor, L. (2020) · Nutrients · doi:10.3390/nu12061899 · Cited by 278 · see citing works

Tricarboxylic acid cycle intermediates in human muscle during prolonged exercise

Sahlin, K., Katz, A., & Broberg, S. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.259.5.c834 · Cited by 274 · see citing works

Skeletal myocytes are a source of interleukin‐6 mRNA expression and protein release during contraction: evidence of fiber type specificity

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

Endocrine 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

Hypoxia-Induced Apelin Expression Regulates Endothelial Cell Proliferation and Regenerative Angiogenesis

Eyries, M., Siegfried, G., Ciumas, M., Montagne, K., Agrapart, M., Lebrin, F., & Soubrier, F. (2008) · Circulation Research · doi:10.1161/circresaha.108.179333 · Cited by 268 · see citing works

Expression of interleukin-15 in human skeletal muscle effect of exercise and muscle fibre type composition

Nielsen, A. R., Mounier, R., Plomgaard, P., Mortensen, O. H., Penkowa, M., Speerschneider, T., Pilegaard, H., & Pedersen, B. K. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.139618 · Cited by 266 · see citing works

Spatial and temporal role of the apelin/APJ system in the caliber size regulation of blood vessels during angiogenesis

Kidoya, H., Ueno, M., Yamada, Y., Mochizuki, N., Nakata, M., Yano, T., Fujii, R., & Takakura, N. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601982 · Cited by 265 · see citing works

Myostatin is a direct regulator of osteoclast differentiation and its inhibition reduces inflammatory joint destruction in mice

Dankbar, B., Fennen, M., Brunert, D., Hayer, S., Frank, S., Wehmeyer, C., Beckmann, D., Paruzel, P., Bertrand, J., Redlich, K., et al. (2015) · Nature Medicine · doi:10.1038/nm.3917 · Cited by 262 · see citing works

Hyperinnervation of Neuromuscular Junctions Caused by GDNF Overexpression in Muscle

Nguyen, Q. T., Parsadanian, A. S., Snider, W. D., & Lichtman, J. W. (1998) · Science · doi:10.1126/science.279.5357.1725 · Cited by 260 · see citing works

Effects of Resistance or Aerobic Exercise Training on Interleukin-6, C-Reactive Protein, and Body Composition

Donges, C. E., Duffield, R., & Drinkwater, E. J. (2010) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181b117ca · Cited by 258 · see citing works

Role of exercise‐induced brain‐derived neurotrophic factor production in the regulation of energy homeostasis in mammals

Pedersen, B. K., Pedersen, M., Krabbe, K. S., Brüünsgaard, H., Matthews, V. B., & Febbraio, M. A. (2009) · Experimental Physiology · doi:10.1113/expphysiol.2009.048561 · Cited by 256 · see citing works

A functional insulin‐like growth factor receptor is not necessary for load‐induced skeletal muscle hypertrophy

Spangenburg, E. E., Roith, D. L., Ward, C. W., & Bodine, S. C. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.141507 · Cited by 251 · see citing works

Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin

Gilson, H., Schakman, O., Kalista, S., Lause, P., Tsuchida, K., & Thissen, J.-P. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00193.2009 · Cited by 248 · see citing works

The Unsolved Enigmas of Leukemia Inhibitory Factor

Metcalf, D. (2003) · Stem Cells · doi:10.1634/stemcells.21-1-5 · Cited by 244 · see citing works

High-intensity interval training evokes larger serum BDNF levels compared with intense continuous exercise

Marquez, C. M. S., Vanaudenaerde, B. M., Troosters, T., & Wenderoth, N. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00126.2015 · Cited by 243 · see citing works

Role of matrix metalloproteinases in skeletal muscle

Chen, X., & Li, Y. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.4.9338 · Cited by 241 · 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

VEGF-A mRNA processing, stability and translation: a paradigm for intricate regulation of gene expression at the post-transcriptional level

Arcondéguy, T., Lacazette, É., Millevoi, S., Prats, H., & Touriol, C. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt539 · Cited by 237 · see citing works

Coupling between Myogenesis and Angiogenesis during Skeletal Muscle Regeneration Is Stimulated by Restorative Macrophages

Latroche, C., Weiss‐Gayet, M., Muller, L., Gitiaux, C., Leblanc, P., Liot, S., Larbi, S. B., Abou-Khalil, R., Verger, N., Bardot, P., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.10.027 · Cited by 234 · see citing works

Effect of endurance training on skeletal muscle myokine expression in obese men: Identification of apelin as a novel myokine

Besse-Patin, A., Montastier, E., Vinel, C., Castan-Laurell, I., Louche, K., Dray, C., Daviaud, D., Mir, L., Marques, M.-A., Thalamas, C., et al. (2014) · International Journal of Obesity · doi:10.1038/ijo.2013.158 · Cited by 227 · see citing works

Cytokines and chemokines are both expressed by human myoblasts: possible relevance for the immune pathogenesis of muscle inflammation.

Rossi, M. D. (2000) · International Immunology · doi:10.1093/intimm/12.9.1329 · Cited by 227 · see citing works

Overexpression of interleukin-15 induces skeletal muscle hypertrophy in vitro: implications for treatment of muscle wasting disorders

Quinn, L. S., Anderson, B. G., Drivdahl, R. H., Alvarez, B., & Argilés, J. M. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5624 · Cited by 226 · see citing works

Apelin Treatment Increases Complete Fatty Acid Oxidation, Mitochondrial Oxidative Capacity, and Biogenesis in Muscle of Insulin-Resistant Mice

Attané, C., Foussal, C., Gonidec, S. L., Bénani, A., Daviaud, D., Wanecq, E., Guzmán‐Ruiz, R., Dray, C., Bézaire, V., Rancoule, C., et al. (2011) · Diabetes · doi:10.2337/db11-0100 · Cited by 226 · 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

Follistatin-mediated skeletal muscle hypertrophy is regulated by Smad3 and mTOR independently of myostatin

Winbanks, C. E., Weeks, K. L., Thomson, R. E., Sepulveda, P. V., Beyer, C., Qian, H., Chen, J. L., Allen, J. M., Lancaster, G. I., Febbraio, M. A., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109091 · Cited by 218 · see citing works

Intrinsic stiffness of extracellular matrix increases with age in skeletal muscles of mice

Wood, L. K., Kayupov, E., Gumucio, J. P., Mendias, C. L., Claflin, D. R., & Brooks, S. V. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00256.2014 · Cited by 212 · see citing works

Apelin (65‐77) activates p70 S6 kinase and is mitogenic for umbilical endothelial cells

Masri, B., Morin, N., Cornu, M., Knibiehler, B., & Audigier, Y. (2004) · The FASEB Journal · doi:10.1096/fj.04-1930fje · Cited by 211 · see citing works

BDNF is expressed in skeletal muscle satellite cells and inhibits myogenic differentiation

Mousavi, K., & Jasmin, B. J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5398-05.2006 · Cited by 210 · 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

Matrix metalloproteinase activity is required for activity-induced angiogenesis in rat skeletal muscle

Haas, T. L., Milkiewicz, M., Davis, S. J., Zhou, A., Egginton, S., Brown, M. D., Madri, J. A., & HUDLICKÁ, O. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.4.h1540 · Cited by 207 · see citing works

Exercise adaptation attenuates VEGF gene expression in human skeletal muscle

Richardson, R. S., Wagner, H. E., Mudaliar, S. R. D., Saucedo, E., Henry, R. R., & Wagner, P. D. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.2.h772 · Cited by 205 · see citing works

MOTS-c Is an Exercise-Induced Mitochondrial-Encoded Regulator of Age-Dependent Physical Decline and Muscle Homeostasis

Reynolds, J. C., Lai, R. W., Woodhead, J. S. T., Joly, J. H., Mitchell, C. J., Cameron-Smith, D., Lu, R., Cohen, P., Graham, N. A., Benayoun, B. A., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20790-0 · Cited by 199 · see citing works

Influence of vitamin C supplementation on oxidative and immune changes after an ultramarathon

Nieman, D. C., Henson, D. A., McAnulty, S. R., McAnulty, L., Swick, N. S., Utter, A. C., Vinci, D. M., Opiela, S. J., & Morrow, J. D. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00961.2001 · Cited by 198 · 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

Carbohydrate ingestion attenuates the increase in plasma interleukin-6, but not skeletal muscle interleukin-6 mRNA, during exercise in humans

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

Viral expression of insulin-like growth factor-I enhances muscle hypertrophy in resistance-trained rats

Lee, S., Barton, E. R., Sweeney, H. L., & Farrar, R. P. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00479.2003 · Cited by 197 · see citing works

Natriuretic peptides enhance the oxidative capacity of human skeletal muscle

Engeli, S., Birkenfeld, A. L., Badin, P.-M., Bourlier, V., Louche, K., Viguerie, N., Thalamas, C., Montastier, É., Larrouy, D., Harant, I., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci64526 · Cited by 197 · see citing works

Effect of Resistance, Endurance, and Concurrent Training on TNF-α, IL-6, and CRP

Libardi, C. A., de Souza, G. V., Cavaglieri, C. R., Madruga, V. A., & Chacon‐Mikahil, M. P. T. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318229d2e9 · Cited by 196 · see citing works

Extracellular Vesicles and Exosomes: Insights From Exercise Science

Nederveen, J. P., Warnier, G., Carlo, A. D., Nilsson, M. I., & Tarnopolsky, M. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.604274 · Cited by 192 · see citing works

Mechanical Signals, IGF-I Gene Splicing, and Muscle Adaptation

Goldspink, G. (2005) · Physiology · doi:10.1152/physiol.00004.2005 · Cited by 191 · see citing works

Myotube-derived exosomal miRNAs downregulate Sirtuin1 in myoblasts during muscle cell differentiation

Forterre, A. V., Jalabert, A., Chikh, K., Pesenti, S., Euthine, V., Granjon, A., Errazuriz, E., Lefai, É., Vidal, H., & Rome, S. (2013) · Cell Cycle · doi:10.4161/cc.26808 · Cited by 191 · see citing works

Myonectin Is an Exercise-Induced Myokine That Protects the Heart From Ischemia-Reperfusion Injury

Otaka, N., Shibata, R., Ohashi, K., Uemura, Y., Kambara, T., Enomoto, T., Ogawa, H., Ito, M., Kawanishi, H., Maruyama, S., et al. (2018) · Circulation Research · doi:10.1161/circresaha.118.313777 · Cited by 189 · see citing works

Macrophage PPARγ, a Lipid Activated Transcription Factor Controls the Growth Factor GDF3 and Skeletal Muscle Regeneration

Varga, T., Mounier, R., Patsalos, A., Gogolák, P., Peloquin, M., Horváth, A., Pap, A., Dániel, B., Nagy, G., Pintye, É., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.10.016 · Cited by 187 · see citing works

Muscle regeneration in the prolonged absence of myostatin

Wagner, K. R., Liu, X., Chang, X., & Allen, R. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408729102 · Cited by 186 · see citing works

Brain-derived Neurotrophic Factor in Megakaryocytes

Chacón-Fernández, P., Säuberli, K., Colzani, M., Moreau, T., Ghevaert, C., & Barde, Y.-A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.720029 · Cited by 186 · see citing works

Advances and challenges in skeletal muscle angiogenesis

Olfert, I. M., Baum, O., Hellsten, Y., & Egginton, S. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00635.2015 · Cited by 185 · see citing works

Mitochondrially derived peptides as novel regulators of metabolism

Kim, S., Xiao, J., Wan, J., Cohen, P., & Yen, K. (2017) · The Journal of Physiology · doi:10.1113/jp274472 · 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

Multiple signaling pathways mediate LIF-induced skeletal muscle satellite cell proliferation

Spangenburg, E. E., & Booth, F. W. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00574.2001 · Cited by 181 · see citing works

Proteomic identification of secreted proteins from human skeletal muscle cells and expression in response to strength training

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

Plasma Metabolome Profiling of Resistance Exercise and Endurance Exercise in Humans

Morville, T. H., Sahl, R. E., Möritz, T., Helge, J. W., & Clemmensen, C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108554 · Cited by 179 · see citing works

Bimagrumab vs Optimized Standard of Care for Treatment of Sarcopenia in Community-Dwelling Older Adults: A Randomized Clinical Trial

Rooks, D., Swan, T., Goswami, B., Filosa, L. A., Bunte, O., Panchaud, N., Coleman, L. A., Miller, R. R., Garcia Garayoa, E., Praestgaard, J., et al. (2020) · JAMA Network Open · doi:10.1001/jamanetworkopen.2020.20836 · Cited by 177 · cited 1× · see citing works

Brain-derived Neurotrophic Factor Regulates Satellite Cell Differentiation and Skeltal Muscle Regeneration

Clow, C., & Jasmin, B. J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0154 · Cited by 175 · see citing works

Meteorin-like facilitates skeletal muscle repair through a Stat3/IGF-1 mechanism

Baht, G., Bareja, A., Lee, D. E., Rao, R. R., Huang, R., Huebner, J., Bartlett, D. B., Hart, C., Gibson, J. R., Lanza, I., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0184-y · Cited by 168 · see citing works

Role of satellite cells versus myofibers in muscle hypertrophy induced by inhibition of the myostatin/activin signaling pathway

Lee, S., Huynh, T. V., Lee, Y., Sebald, S. M., Wilcox‐Adelman, S. A., Iwamori, N., Lepper, C., Matzuk, M. M., & Fan, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206410109 · Cited by 167 · see citing works

Influence of carbohydrate ingestion on immune changes after 2 h of intensive resistance training

Nieman, D. C., Davis, J. M., Brown, V. A., Henson, D. A., Dumke, C. L., Utter, A. C., Vinci, D. M., Downs, M. F., Smith, J., Carson, J. A., et al. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01064.2003 · Cited by 166 · see citing works

Effects of prolonged strenuous exercise on plasma levels of atrial natriuretic peptide and brain natriuretic peptide in healthy men

Ohba, H., 高田, 英., Musha, H., Nagashima, J., Mori, N., Awaya, T., Omiya, K., & Murayama, M. (2001) · American Heart Journal · doi:10.1067/mhj.2001.114371 · 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

Myokines mediate the cross talk between skeletal muscle and other organs

Chen, W., Wang, L., You, W., & Shan, T. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30033 · Cited by 162 · see citing works

Effects of systemic hypoxia on human muscular adaptations to resistance exercise training

Kon, M., Ohiwa, N., Honda, A., Matsubayashi, T., Ikeda, T., Akimoto, T., Suzuki, Y., Hirano, Y., & Russell, A. P. (2014) · Physiological Reports · doi:10.14814/phy2.12033 · Cited by 161 · see citing works

Myogenic Akt Signaling Regulates Blood Vessel Recruitment during Myofiber Growth

Takahashi, A., Kureishi, Y., Jiang, Y., Luo, Z., Guo, K. Y., Mukhopadhyay, D., Ivashchenko, Y., Branellec, D., & Walsh, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4803-4814.2002 · Cited by 159 · see citing works

Exercise-Released Myokines in the Control of Energy Metabolism

Laurens, C., Bergouignan, A., & Moro, C. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00091 · 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

Integrin signaling: linking mechanical stimulation to skeletal muscle hypertrophy

Boppart, M. D., & Mahmassani, Z. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00009.2019 · Cited by 157 · see citing works

Cytokine gene expression in human skeletal muscle during concentric contraction: evidence that IL-8, like IL-6, is influenced by glycogen availability

Chan, S. M. H., Carey, A. L., Watt, M. J., & Febbraio, M. A. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00030.2004 · Cited by 156 · see citing works

IL-6 Induced STAT3 Signalling Is Associated with the Proliferation of Human Muscle Satellite Cells Following Acute Muscle Damage

Toth, K., McKay, B. R., Lisio, M. D., Little, J. P., Tarnopolsky, M. A., & Parise, G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017392 · Cited by 155 · see citing works

LIF is a contraction-induced myokine stimulating human myocyte proliferation

Broholm, C., Laye, M. J., Brandt, C., Vadalasetty, R., Pilegaard, H., Pedersen, B. K., & Scheele, C. C. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01399.2010 · Cited by 155 · see citing works

Delivery of muscle-derived exosomal miRNAs induced by HIIT improves insulin sensitivity through down-regulation of hepatic FoxO1 in mice

Castaño, C., Mirasierra, M., Vallejo, M., Novials, A., & Párrizas, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016112117 · Cited by 154 · see citing works

Apelin, a promising target for type 2 diabetes treatment?

Castan‐Laurell, I., Dray, C., Knauf, C., Kunduzova, O., & Valet, P. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.02.005 · Cited by 150 · see citing works

Association of Interleukin-6 Signalling with the Muscle Stem Cell Response Following Muscle-Lengthening Contractions in Humans

McKay, B. R., De Lisio, M., Johnston, A. P. W., O'Reilly, C. E., Phillips, S. M., Tarnopolsky, M. A., & Parise, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006027 · Cited by 149 · see citing works

Muscle-derived interleukin 6 increases exercise capacity by signaling in osteoblasts

Chowdhury, S., Schulz, L., Palmisano, B., Singh, P. P., Berger, J. M., Yadav, V. K., Mera, P., Ellingsgaard, H., Hidalgo, J., Brüning, J. C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133572 · Cited by 148 · see citing works

The skeletal muscle secretome: an emerging player in muscle–bone crosstalk

Hamrick, M. W. (2012) · BoneKEy Reports · doi:10.1038/bonekey.2012.60 · Cited by 145 · see citing works

Interaction of contractile activity and training history on mRNA abundance in skeletal muscle from trained athletes

Coffey, V. G., SHIELD, A. J., Canny, B. J., Carey, K. A., Cameron‐Smith, D., & Hawley, J. A. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00299.2005 · Cited by 144 · see citing works

BDNF is a mediator of glycolytic fiber-type specification in mouse skeletal muscle

Delezie, J., Weihrauch, M., Maier, G., Tejero, R., Ham, D. J., Gill, J. F., Karrer-Cardel, B., Rüegg, M. A., Tabares, L., & Handschin, C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900544116 · 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

Mitochondrial-derived peptides in energy metabolism

Merry, T. L., Chan, A., Woodhead, J. S. T., Reynolds, J. C., Kumagai, H., Kim, S.-J., & Lee, C. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00249.2020 · Cited by 141 · see citing works

Interleukin-13 drives metabolic conditioning of muscle to endurance exercise

Knudsen, N. H., Stanya, K. J., Hyde, A. L., Chalom, M. M., Alexander, R. K., Liou, Y.-H., Starost, K. A., Gangl, M. R., Jacobi, D., Liu, S., et al. (2020) · Science · doi:10.1126/science.aat3987 · Cited by 139 · see citing works

Coordinated Vascular Endothelial Growth Factor Expression and Signaling During Skeletal Myogenic Differentiation

Bryan, B. A., Walshe, T. E., Mitchell, D., Havumaki, J. S., Saint‐Geniez, M., Maharaj, A. S. R., Maldonado, A. E., & D'Amore, P. A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0856 · Cited by 138 · see citing works

Succinate induces skeletal muscle fiber remodeling via SUCNR1 signaling

Wang, T., Xu, Y., Yuan, Y., Xu, P., Zhang, C., Li, F., Wang, L., Yin, C., Zhang, L., Cai, X., et al. (2019) · EMBO Reports · doi:10.15252/embr.201947892 · Cited by 137 · see citing works

SPARC Inhibits Adipogenesis by Its Enhancement of β-Catenin Signaling

Nie, J., & Sage, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808285200 · Cited by 136 · see citing works

Retardation of Retinal Vascular Development in Apelin-Deficient Mice

Kasai, A., Shintani, N., Kato, H., Matsuda, S., Gomi, F., Haba, R., Hashimoto, H., Kakuda, M., Tano, Y., & Baba, A. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.163402 · Cited by 136 · see citing works

Role of mTORC1 in mechanically induced increases in translation and skeletal muscle mass

Goodman, C. A. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01011.2018 · Cited by 133 · see citing works

Exercise and cardiac health: physiological and molecular insights

Moreira, J. B. N., Wohlwend, M., & Wisløff, U. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0262-1 · Cited by 132 · see citing works

Apelin signaling drives vascular endothelial cells toward a pro-angiogenic state

Helker, C. S., Eberlein, J., Wilhelm, K., Sugino, T., Malchow, J., Schuermann, A., Baumeister, S., Kwon, H.-B., Maischein, H., Potente, M., et al. (2020) · eLife · doi:10.7554/elife.55589 · Cited by 132 · see citing works

The ABCs of IGF-I isoforms: impact on muscle hypertrophy and implications for repair

Barton, E. R. (2006) · Applied Physiology Nutrition and Metabolism · doi:10.1139/h06-054 · Cited by 126 · see citing works

Succinate accumulation in man during exercise

Hochachka, P. W., & Dressendorfer, R. H. (1976) · European Journal of Applied Physiology · doi:10.1007/bf00423282 · Cited by 125 · see citing works

Circulating follistatin is liver-derived and regulated by the glucagon-to-insulin ratio

Hansen, J. S., Rutti, S., Arous, C., Clemmesen, J. O., Secher, N. H., Drescher, A., Gonelle-Gispert, C., Halban, P. A., Pedersen, B. K., Weigert, C., et al. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3668 · Cited by 125 · see citing works

Acute resistance exercise increases skeletal muscle angiogenic growth factor expression

Gavin, T. P., Drew, J. L., Kubik, C. J., Pofahl, W. E., & Hickner, R. C. (2007) · Acta Physiologica · doi:10.1111/j.1748-1716.2007.01723.x · Cited by 124 · see citing works

Early Activation of Rat Skeletal Muscle IL-6/STAT1/STAT3 Dependent Gene Expression in Resistance Exercise Linked to Hypertrophy

Begue, G., Douillard, A., Galbes, O., Rossano, B., Vernus, B., Candau, R., & Py, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057141 · Cited by 124 · see citing works

Apelin/APJ signaling system: a potential link between adipose tissue and endothelial angiogenic processes

Kunduzova, O., Alet, N., Delesque-Touchard, N., Millet, L., Castan‐Laurell, I., Muller, C., Dray, C., Schaeffer, P., Hérault, J. P., Savi, P., et al. (2008) · The FASEB Journal · doi:10.1096/fj.07-104018 · Cited by 123 · see citing works

Myostatin inhibition induces muscle fibre hypertrophy prior to satellite cell activation

Wang, Q., & McPherron, A. C. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2011.226001 · Cited by 122 · see citing works

Increased bone mineral density in the femora of GDF8 knockout mice

Hamrick, M. W. (2003) · The Anatomical Record Part A Discoveries in Molecular Cellular and Evolutionary Biology · doi:10.1002/ar.a.10044 · Cited by 121 · see citing works

Skeletal Muscle-derived Myonectin Activates the Mammalian Target of Rapamycin (mTOR) Pathway to Suppress Autophagy in Liver

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

Differential adaptation of growth and differentiation factor 8/myostatin, fibroblast growth factor 6 and leukemia inhibitory factor in overloaded, regenerating and denervated rat muscles

Sakuma, K., Watanabe, K., Sano, M., Uramoto, I., & Totsuka, T. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00044-6 · Cited by 120 · see citing works

STAT3 signaling is activated in human skeletal muscle following acute resistance exercise

Caldow, M. K., Carey, K. A., Ward, A. C., & Cameron‐Smith, D. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01147.2006 · Cited by 118 · see citing works

MicroRNA transcriptome profiles during swine skeletal muscle development

McDaneld, T. G., Smith, T. P. L., Doumit, M. E., Miles, J. R., Coutinho, L. L., Sonstegard, T. S., Matukumalli, L. K., Nonneman, D., & Wiedmann, R. T. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-77 · Cited by 117 · see citing works

The Copper Binding Domain of SPARC Mediates Cell Survival in Vitro via Interaction with Integrin β1 and Activation of Integrin-linked Kinase

Weaver, M. S., Workman, G. A., & Sage, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706563200 · Cited by 113 · see citing works

PGC-1α Induces SPP1 to Activate Macrophages and Orchestrate Functional Angiogenesis in Skeletal Muscle

Rowe, G. C., Raghuram, S., Jang, C., Nagy, J. A., Patten, I. S., Goyal, A., Chan, M. C., Liu, L. X., Jiang, A., Spokes, K., et al. (2014) · Circulation Research · doi:10.1161/circresaha.115.303829 · Cited by 112 · see citing works

Temporal alterations in protein signaling cascades during recovery from muscle atrophy

Childs, T. E., Spangenburg, E. E., Vyas, D. R., & Booth, F. W. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00478.2002 · Cited by 112 · see citing works

Resistance exercise-induced changes of inflammatory gene expression within human skeletal muscle

Buford, T. W., Cooke, M. B., & Willoughby, D. S. (2009) · European Journal of Applied Physiology · doi:10.1007/s00421-009-1145-z · Cited by 111 · see citing works

A myostatin and activin decoy receptor enhances bone formation in mice

Bialek, P., Parkington, J. D., Li, X., Gavin, D., Wallace, C. E., Zhang, J., Root, A. R., Yan, G., Warner, L., Seeherman, H. J., et al. (2013) · Bone · doi:10.1016/j.bone.2013.12.002 · Cited by 111 · see citing works

Regulation of follistatin-like protein 1 expression and secretion in primary human skeletal muscle cells

Görgens, S. W., Raschke, S., Holven, K. B., Jensen, J., Eckardt, K., & Eckel, J. (2013) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2013.768270 · Cited by 109 · see citing works

Exercise but not Prostanoids Enhance Levels of Vascular Endothelial Growth Factor and other Proliferative Agents in Human Skeletal Muscle Interstitium

Höffner, L., Nielsen, J., Langberg, H., & Hellsten, Y. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.037051 · Cited by 108 · see citing works

Contraction-induced interleukin-6 gene transcription in skeletal muscle is regulated by c-Jun terminal kinase/activator protein-1

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

Exercise induces interleukin‐8 receptor (CXCR2) expression in human skeletal muscle

Frydelund‐Larsen, L., Penkowa, M., Akerstrom, T., Zankari, A., Nielsen, S., & Pedersen, B. K. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2006.034769 · Cited by 106 · see citing works

Skeletal Muscle Mass Recovery from Atrophy in IL-6 Knockout Mice

Washington, T. A., White, J., Davis, J. M., Wilson, L., Lowe, L. L., Sato, S., & Carson, J. A. (2011) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02281.x · Cited by 106 · see citing works

Effect of exercise training on skeletal muscle cytokine expression in the elderly

Gatta, P. A. D., GARNHAM, A. P., Peake, J. M., & Cameron‐Smith, D. (2014) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2014.01.006 · Cited by 101 · see citing works

Resistance exercise increases NF-κB activity in human skeletal muscle

Vella, L. D., Caldow, M. K., Larsen, A., Tassoni, D., Gatta, P. A. D., Gran, P., Russell, A. P., & Cameron‐Smith, D. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00336.2011 · Cited by 98 · see citing works

Neuromuscular Junction Disassembly and Muscle Fatigue in Mice Lacking Neurotrophin-4

Belluardo, N., Westerblad, H., Mudò, G., Casabona, A., Bruton, J. D., Caniglia, G., Pastoris, O., Grassi, F., & Ibáñez, C. F. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.1001 · Cited by 98 · see citing works

Updated overview on interplay between physical exercise, neurotrophins, and cognitive function in humans

Lippi, G., Mattiuzzi, C., & Sanchis‐Gomar, F. (2019) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2019.07.012 · Cited by 98 · see citing works

GLP-1 secretion is regulated by IL-6 signalling: a randomised, placebo-controlled study

Ellingsgaard, H., Seelig, E., Timper, K., Coslovsky, M., Soederlund, L., Lyngbæk, M. P. P., Albrechtsen, N. J. W., Schmidt‐Trucksäss, A., Hanssen, H., Frey, W. O., et al. (2019) · Diabetologia · doi:10.1007/s00125-019-05045-y · Cited by 96 · see citing works

Muscle Wasting Diseases: Novel Targets and Treatments

Furrer, R., & Handschin, C. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021041 · Cited by 93 · see citing works

Skeletal muscle‐derived exosomes regulate endothelial cell functions via reactive oxygen species‐activated nuclear factor‐κB signalling

Nie, Y., Sato, Y., Garner, R. T., Kargl, C. K., Wang, C., Kuang, S., Gilpin, C. J., & Gavin, T. P. (2019) · Experimental Physiology · doi:10.1113/ep087396 · Cited by 93 · see citing works

Exerkines in health, resilience and disease

Chow, L. S., Gerszten, R. E., Taylor, J. M., Pedersen, B. K., van Praag, H., Trappe, S., Febbraio, M. A., Galis, Z. S., Gao, Y., Haus, J. M., et al. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00641-2 · Cited by 927 · see citing works

Molecular Responses to Acute Exercise and Their Relevance for Adaptations in Skeletal Muscle to Exercise Training

Egan, B., & Sharples, A. P. (2023) · Physiological Reviews · doi:10.1152/physrev.00054.2021 · Cited by 278 · see citing works

Exercise benefits in cardiovascular diseases: From mechanisms to clinical implementation

Valenzuela, P. L., Ruilope, L. M., Santos-Lozano, A., Wilhelm, M., Kränkel, N., Fiuza-Luces, C., & Lucia, A. (2023) · European Heart Journal · doi:10.1093/eurheartj/ehad170 · Cited by 237 · 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

Neuroprotective mechanisms of exercise and the importance of fitness for healthy brain ageing

Tari, A. R., Walker, T. L., Huuha, A. M., Sando, S. B., & Wisløff, U. (2025) · The Lancet · doi:10.1016/s0140-6736(25)00184-9 · Cited by 174 · see citing works

Exercise therapy for people with sarcopenic obesity: myokines and adipokines as effective actors

Alizadeh Pahlavani, H. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.811751 · Cited by 145 · see citing works

Exercise Induces Tissue-Specific Adaptations to Enhance Cardiometabolic Health

Ashcroft, S. P., Stocks, B., Egan, B., & Zierath, J. R. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2023.12.008 · Cited by 149 · see citing works

Molecular control of endurance training adaptation in male mouse skeletal muscle

Furrer, R., Heim, B., Schmid, S., Dilbaz, S., Adak, V., Nordström, K. J. V., Ritz, D., Steurer, S. A., Walter, J., & Handschin, C. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00891-y · Cited by 68 · see citing works

Isolation of extracellular fluids reveals novel secreted bioactive proteins from muscle and fat tissues

Mittenbühler, M. J., Jedrychowski, M. P., Vranken, J. G. V., Sprenger, H., Wilensky, S. E., Dumesic, P. A., Sun, Y., Tartaglia, A., Laznik-Bogoslavski, D., Mu, A., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2022.12.014 · Cited by 66 · 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

Organokines, Sarcopenia, and Metabolic Repercussions: The Vicious Cycle and the Interplay with Exercise

Minniti, G., Pescinini-Salzedas, L. M., Minniti, G. A. D. S., Laurindo, L. F., Barbalho, S. M., Sinatora, R. V., Sloan, L. A., Haber, R. S. D. A., Araújo, A. C., Quesada, K. R., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113452 · Cited by 52 · see citing works

Examining the Interaction between Exercise, Gut Microbiota, and Neurodegeneration: Future Research Directions

Rojas‐Valverde, D., Bonilla, D. A., Gómez-Miranda, L. M., Calleja-Núñez, J. J., Arias, N., & Martínez‐Guardado, I. (2023) · Biomedicines · doi:10.3390/biomedicines11082267 · Cited by 42 · see citing works

Skeletal Muscle as a Mediator of Interorgan Crosstalk During Exercise: Implications for Aging and Obesity

Shero, J. A., Lindholm, M. E., Sandri, M. F., & Stanford, K. I. (2025) · Circulation Research · doi:10.1161/circresaha.124.325614 · Cited by 43 · see citing works

Exercise, exerkines, and cardiometabolic health: from individual players to a team sport

Robbins, J., & Gerszten, R. E. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168121 · Cited by 41 · see citing works

‘Exerkines’: A Comprehensive Term for the Factors Produced in Response to Exercise

Novelli, G., Calcaterra, G., Casciani, F., Pecorelli, S., & Mehta, J. L. (2024) · Biomedicines · doi:10.3390/biomedicines12091975 · Cited by 34 · see citing works

Musculoskeletal Deficits and Cognitive Impairment: Epidemiological Evidence and Biological Mechanisms

Sui, S. X., Balanta‐Melo, J., Pasco, J. A., & Plotkin, L. I. (2022) · Current Osteoporosis Reports · doi:10.1007/s11914-022-00736-9 · Cited by 34 · see citing works

Interleukin‐6 potentiates endurance training adaptation and improves functional capacity in old mice

Leuchtmann, A. B., Furrer, R., Steurer, S. A., Schneider‐Heieck, K., Karrer‐Cardel, B., Sagot, Y., & Handschin, C. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12949 · Cited by 29 · see citing works

Aging, Osteo-Sarcopenia, and Musculoskeletal Mechano-Transduction

Leser, J. M., Harriot, A. D., Buck, H., Ward, C. W., & Stains, J. P. (2021) · Frontiers in Rehabilitation Sciences · doi:10.3389/fresc.2021.782848 · Cited by 28 · see citing works

Mustn1 is a smooth muscle cell-secreted microprotein that modulates skeletal muscle extracellular matrix composition

Ducommun, S., Jannig, P. R., Červenka, I., Murgia, M., Mittenbühler, M. J., Chernogubova, E., Dias, J. M. M., Jude, B., Correia, J. C., Vranken, J. G. V., et al. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.101912 · Cited by 25 · see citing works

Cellular deconstruction of the human skeletal muscle microenvironment identifies an exercise-induced histaminergic crosstalk

der Stede, T. V., de Loock, A. V., Turiel, G., Hansen, C. C., Tamariz‐Ellemann, A., Ullrich, M., Lievens, E., Spaas, J., Yigit, N., Anckaert, J., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2024.12.011 · Cited by 25 · see citing works

Acetate and succinate benefit host muscle energetics as exercise‐associated post‐biotics

Ismaeel, A., Valentino, T. R., Burke, B. I., Goh, J. Z., Saliu, T. P., Albathi, F. A., Owen, A. M., McCarthy, J. J., & Wen, Y. (2023) · Physiological Reports · doi:10.14814/phy2.15848 · Cited by 24 · see citing works

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Dowling, P., Swandulla, D., & Ohlendieck, K. (2023) · Cells · doi:10.3390/cells12212560 · Cited by 18 · see citing works

Loss of association between plasma irisin levels and cognition in Alzheimer’s disease

Kim, K. Y., Kwak, S., Ha, J., Oh, D. J., Kim, M., Cho, S. Y., Kim, H., Lee, J., & Kim, E. (2021) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2021.105624 · Cited by 22 · see citing works

Pharmacological and exercise‐induced activation of AMPK as emerging therapies for myotonic dystrophy type 1 patients

Ravel‐Chapuis, A., Duchesne, É., & Jasmin, B. J. (2022) · The Journal of Physiology · doi:10.1113/jp282725 · Cited by 19 · see citing works

Exploiting the therapeutic potential of contracting skeletal muscle-released extracellular vesicles in cancer: Current insights and future directions

Pinto, A. C., Tavares, P., Neves, B. M., Oliveira, P. F., Vitorino, R. M. P., Moreira‐Gonçalves, D., & Ferreira, R. M. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-024-02427-7 · Cited by 18 · see citing works

Microgravity accelerates skeletal muscle degeneration: Functional and transcriptomic insights from an ISS muscle lab-on-chip model

Parafati, M., Thwin, Z., Malany, L. K., Coen, P. M., & Malany, S. (2025) · Stem Cell Reports · doi:10.1016/j.stemcr.2025.102550 · Cited by 15 · see citing works

The Role of miRNAs and Extracellular Vesicles in Adaptation After Resistance Exercise: A Review

Csala, D., Ádám, Z., & Wilhelm, M. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47080583 · Cited by 16 · see citing works

Effects of acute and chronic high-intensity interval training on serum irisin, BDNF and apelin levels in male soccer referees

Küçük, H., Söyler, M., Ceylan, T., Ceylan, L., & Şahin, F. N. (2024) · Journal of Men s Health · doi:10.22514/jomh.2024.027 · Cited by 15 · see citing works

Dynamic of irisin secretion change after moderate-intensity chronic physical exercise on obese female

Merawati, D., Sugiharto, S., Susanto, H., Taufiq, A., Pranoto, A., Amelia, D., & Rejeki, P. S. (2023) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2023-0041 · Cited by 14 · see citing works

Post-natal muscle growth and protein turnover: a narrative review of current understanding

Millward, D. J. (2023) · Nutrition Research Reviews · doi:10.1017/s0954422423000124 · Cited by 14 · see citing works

Association of physical activity and trajectories of physical activity with cardiovascular disease

Chrysant, S. G., & Chrysant, G. S. (2023) · Expert Review of Cardiovascular Therapy · doi:10.1080/14779072.2023.2174102 · Cited by 13 · see citing works

Myokines as potential mediators of changes in glucose homeostasis and muscle mass after bariatric surgery

Orioli, L., & Thissen, J. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1554617 · Cited by 13 · see citing works

Exercise-Boosted Mitochondrial Remodeling in Parkinson’s Disease

Magaña, J. C., Deus, C. M., Giné‐Garriga, M., Montané, J., & Pereira, S. P. (2022) · Biomedicines · doi:10.3390/biomedicines10123228 · Cited by 15 · see citing works

Eight weeks of combined exercise training do not alter circulating microRNAs-29a, -133a, -133b, and -155 in young, healthy men

Meza, C. A., Amador, M., McAinch, A. J., Begum, K., Roy, S., & Bajpeyi, S. (2022) · European Journal of Applied Physiology · doi:10.1007/s00421-022-04886-7 · Cited by 12 · see citing works

Stubborn Exercise Responders–Where to Next?

Bell, L. R., Gabbett, T. J., Davis, G. M., Wallen, M. P., & O’Brien, B. J. (2022) · Sports · doi:10.3390/sports10060095 · Cited by 12 · see citing works

Charting the Molecular Terrain of Exercise: Energetics, Exerkines, and the Future of Multiomic Mapping

Katz, D. H., Lindholm, M. E., & Ashley, E. A. (2024) · Physiology · doi:10.1152/physiol.00024.2024 · Cited by 12 · see citing works

Musclin prevents depression-like behavior in male mice by activating urocortin 2 signaling in the hypothalamus

Ataka, K., Asakawa, A., Iwai, H., & Kato, I. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1288282 · Cited by 11 · see citing works

Study on Anti-Inflammatory Effects of and Muscle Recovery Associated with Transdermal Delivery of Chaenomeles speciosa Extracts Using Supersonic Atomizer on Rat Model

Hsieh, T.-J., Chen, P., Wang, H.-Y., Wu, C.-S., Liu, L.-F., Wu, K.-L., & Kuo, S. (2024) · Antioxidants · doi:10.3390/antiox13060702 · Cited by 9 · see citing works

Exploring the Impact of Exercise-Derived Extracellular Vesicles in Cancer Biology

Silvestri, M., Grazioli, E., Duranti, G., Sgrò, P., & Dimauro, I. (2024) · Biology · doi:10.3390/biology13090701 · Cited by 9 · see citing works

Physical exercise for treating non-motor symptoms assessed by general Parkinson’s disease scales: systematic review and meta-analysis of clinical trials

Costa, V., Suassuna, A. D. O. B., Brito, T. S. S., da Rocha, T. F., & Gianlorenço, A. C. (2023) · BMJ Neurology Open · doi:10.1136/bmjno-2023-000469 · Cited by 9 · see citing works

Changes in body composition, muscle function, and muscle insulin sensitivity induced by obesity and bariatric surgery: Implications for sarcopenic obesity

Orioli, L., Thissen, J.-P., & Loumaye, A. (2025) · Clinical Nutrition · doi:10.1016/j.clnu.2025.106547 · Cited by 9 · see citing works

How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?

Dowling, P., Trollet, C., Négroni, E., Swandulla, D., & Ohlendieck, K. (2024) · Proteomes · doi:10.3390/proteomes12010004 · Cited by 9 · see citing works

Pathophysiology of Physical Exercise in Kidney Patients: Unveiling New Players – The Role of Myokines

Picciotto, D., Macciò, L., Verzola, D., Baciga, F., Momentè, C., Russo, E., Viazzi, F. C., Battaglia, Y., & Esposito, P. B. (2024) · Kidney & Blood Pressure Research · doi:10.1159/000539489 · Cited by 8 · see citing works

The Potential of Exerkines in Women’s COVID-19: A New Idea for a Better and More Accurate Understanding of the Mechanisms behind Physical Exercise

Suzuki, K., Hekmatikar, A. H. A., Jalalian, S., Abbasi, S., Ahmadi, E., Kazemi, A., Ruhee, R. T., & Khoramipour, K. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph192315645 · Cited by 8 · see citing works

Health benefits of physical activity: What role does skeletal muscle-organ crosstalk play?

Powers, S. K., Goldstein, E. R., Lategan-Potgieter, R., Schrager, M. A., Skelton, M., & Demirel, H. A. (2025) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2025.02.010 · Cited by 7 · see citing works

High-intensity combination exercise has the highest effect on increasing serum irisin and interleukin 6 levels in women with obesity

Hasanah, U., Rejeki, P. S., Wungu, C. D. K., Pranoto, A., Izzatunnisa, N., Rahmanto, I., & Halim, S. (2024) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2023-0150 · Cited by 6 · see citing works

Research progress on resistance exercise therapy for improving cognitive function in patients with AD and muscle atrophy

Li, W., Fang, W. J., Zhang, Y., Chen, Q., Shentu, W., Lai, Q., Cheng, L., Yan, S., Kong, Q., & Qiao, S. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1552905 · Cited by 5 · see citing works

Amino acid neurotransmitters in sarcopenia and healthy aging

Jonk, S. M., Tribble, J. R., Swoboda, P., & Williams, P. A. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111437 · Cited by 5 · see citing works

Investigating the impact of physical activity on mitochondrial function in Parkinson’s disease (PARKEX): Study protocol for A randomized controlled clinical trial

Magaña, J. C., Deus, C. M., Baldellou, L., Avellanet, M., Gea, E., Enríquez-Calzada, S., Laguna, A., Martínez‐Vicente, M., Hernández‐Vara, J., Giné‐Garriga, M., et al. (2023) · PLoS ONE · doi:10.1371/journal.pone.0293774 · Cited by 5 · see citing works

A critical examination of sport discipline typology: identifying inherent limitations and deficiencies in contemporary classification systems

Konopka, M. J., KEIZER, H. A., Rietjens, G. J., Zeegers, M. P., & Sperlich, B. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1389844 · Cited by 5 · see citing works

Enhanced secretion of promyogenic exosomes by quiescent muscle cells

Prabhavathy, D., Ghosh, A., Pallavi Rao, T., Raychaudhuri, S., Adicherla, H., Devvanshi, H., Kshetrapal, P., & Dhawan, J. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1381357 · Cited by 4 · see citing works

Separate and Combined Effects of Moderate-Intensity Exercise Training and Detraining with Protocatechuic Acid (PCA) on Myokines and Insulin-Signaling Pathways in Male Wistar Rats: A Preclinical Randomized Study

Shakoor, H. I., Kizhakkayil, J., Statsenko, Y. A., & Platat, C. (2025) · Metabolites · doi:10.3390/metabo15020087 · Cited by 4 · see citing works

Are Aminoglycoside Antibiotics TRPing Your Metabolic Switches?

Franco‐Obregón, A., & Tai, Y. K. (2024) · Cells · doi:10.3390/cells13151273 · Cited by 4 · see citing works

Can systemic myokine response to an acute exercise bout predict high and low responders to resistance training?

Bell, L. R., Wallen, M. P., Talpey, S., & O’Brien, B. J. (2022) · Medical Hypotheses · doi:10.1016/j.mehy.2022.110780 · Cited by 4 · see citing works

Exercise modulates redox homeostasis in cardiovascular and metabolic diseases: from bench to clinic

Wang, J., Zhang, J., Zhang, H., Yu, F., Tian, Z., & Jia, D. (2026) · Cardiovascular Diabetology · doi:10.1186/s12933-026-03131-1 · Cited by 3 · see citing works

Effect of combined aerobic-resistance training on regulating adipokine levels among obese females

Sugiharto, S., Rejeki, P. S., Lesmana, R., Merawati, D., Susanto, H., Taufiq, A., Widyatama, F. S., Amelia, D., & Pranoto, A. (2024) · Comparative Exercise Physiology · doi:10.1163/17552559-20231010 · Cited by 3 · see citing works

Impact of BMI and Cardiorespiratory Fitness on Oxidative Stress in Plasma and Circulating Exosomes Following Acute Exercise

Slusher, A. L., Visavadiya, N. P., Fico, B. G., Estébanez, B., Acevedo, E. O., & Huang, C. (2024) · Biology · doi:10.3390/biology13080599 · Cited by 2 · see citing works

Therapeutic potential of exerkines in neurodegenerative and mental disorders: a narrative review

Yang, S., Sang, H.-W., Kim, S., Cho, E., Choi, Y., Kang, D., Jang, Y. C., Park, D.-H., Kwak, H., & Yook, J. S. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1793043 · Cited by 2 · see citing works

The hallmarks of skeletal muscle health

Vainshtein, A., Blaauw, B., Bock, K. D., Muñoz‐Cánoves, P., Olson, E. N., Ottenheijm, C. A. C., Richter, E. A., Ruas, J. L., Schaeffer, L., Spiegelman, B. M., et al. (2026) · Nature Metabolism · doi:10.1038/s42255-026-01595-9 · Cited by 3 · see citing works

Advancing cancer cachexia diagnosis with -omics technology and exercise as molecular medicine

Hesketh, S. J. (2024) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2024.01.006 · Cited by 2 · see citing works

Prescription and physical activity counseling in primary care

Palomeque, G. A. E. (2024) · Gaceta Médica de Caracas · doi:10.47307/gmc.2024.132.1.16 · Cited by 2 · see citing works

Preclinical assessment of the selective androgen receptor modulator RAD140 to increase muscle mass and bone mineral density

Puskas, J., Guda, T., Niccoli, S., Rathbone, C. R., Tan‐Johnson, B., Puskas, D., Middleton, R., Otis, J. S., & Lees, S. J. (2025) · Physiological Reports · doi:10.14814/phy2.70463 · Cited by 2 · see citing works

Injuries in Artistic Gymnastics: Etiology, Prevention Strategies, and Multifactorial Perspectives—A Systematic Review

Mekić, R., Milić, V., Radenković, O., Čaprić, I., Veličković, S., Mujanović, R., Biševac, E., Mahmutović, E., Salihagić, Z., Ajdinović, A., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210929 · Cited by 2 · see citing works

The Influence of Nicotine on Trophoblast-Derived Exosomes in a Mouse Model of Pathogenic Preeclampsia

Kubo, A., Matsubara, K., Matsubara, Y., Nakaoka, H., & Sugiyama, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311126 · Cited by 1 · see citing works

Physical exercise and sarcopenia in older people: an OrtoMed position paper

Moretti, A., Tomaino, F., Paoletta, M., Liguori, S., Migliaccio, S., Iorio, A. D., Pellegrino, R., Donnarumma, D., Nunzio, D. D., Toro, G., et al. (2025) · International Journal of Bone Fragility · doi:10.57582/ijbf.240403.080 · Cited by 1 · see citing works

The long non-coding RNA landscape of endurance exercise training

Bonilauri, B., Smith, G. R., Raja, A. N., Jimenez‐Morales, D., Ahmed, A., Jin, C. A., Sparks, L. M., Walsh, M. J., Montgomery, S. B., Adkins, J. N., et al. (2026) · Molecular Metabolism · doi:10.1016/j.molmet.2026.102358 · Cited by 1 · see citing works

Systemic MOTS-c levels are increased in adults with obesity in association with metabolic dysregulation and remain unchanged after weight loss

Yoon, S.-H., Fei, Y., Zhu, X., Tang, H., Abdurakhimova, D. A., Krier, J. D., Eirin, A., Lerman, A., Cohen, P., & Lerman, L. O. (2025) · Journal of Clinical & Translational Endocrinology · doi:10.1016/j.jcte.2025.100429 · Cited by 1 · see citing works

The Gut–Brain–Muscle Axis: Microbial Regulation of Neuromuscular Aging and Cognitive Frailty

Taslim, N. A., Sibarani, J. N., Alfaray, R. I., Mayulu, N., Mustika, A., Kumalawati, D. A., Permatasari, H. K., Tjandrawinata, R. R., & Nurkolis, F. (2026) · Microorganisms · doi:10.3390/microorganisms14061366 · Cited by 1 · see citing works

Molecular control of endurance training adaptation in mouse skeletal musclePreprint

Furrer, R., Heim, B., Schmid, S., Nordström, K. J. V., Dilbaz, S., Ritz, D., Adak, V., Steurer, S. A., Walter, J., & Handschin, C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.18.529055 · Cited by 1 · see citing works

Cardiomyocyte PGC-1α enables physiological adaptations to endurance exercise through suppression of GDF15 and cardiac atrophyPreprint

Khetarpal, S. A., Li, H., Vitale, T., Rhee, J., Grauvogel, L., Castro, C., Mittenbühler, M. J., Houstis, N. E., Vargas‐Castillo, A., Smythers, A. L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.30.578093 · Cited by 1 · see citing works

Effects of Extreme Physical and Mental Load on Circulating Exerkines in Professional Athletes

Ligetvári, R. (2024) · doi:10.15170/pte.2024.013

Myokines — the cardiometabolic risk potential biomarkers

Timofeev, Y. S., Metelskaya, V. A., Sheptulina, A. F., Neshkova, E. A., Dubovskaya, N. I., Yafarova, A. A., Мамутовна, М. Э., Валерьевна, Д. Н., Khatri, D. N., & Drapkina, O. M. (2025) · Russian Journal of Preventive Medicine · doi:10.17116/profmed202528071119

Muscle Fiber- and Cell Type-Specificity of Training Adaptation in Male MicePreprint

Dilbaz, S., Baraldo, M., Škrinjar, P., Furrer, R., Adak, V., Stein, A., Steurer, S. A., Santos, G., & Handschin, C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.04.686534

Physical activity is associated with a lower risk of pre-sarcopenic obesity in adolescents: evidence from Northwest China

Xu, Y., 石龙凯, Chen, L., Liu, J., & Ding, W. (2025) · Scientific Reports · doi:10.1038/s41598-025-28449-w

MUSTN1 prevents muscle atrophy through ferroptosis suppression: A ACO1-dependent and exosome-mediated mechanism

Hu, Z., Xu, H., Wang, X., Deng, Q., Dai, J., Lu, Y., Chen, J., Liu, Y., Yang, C., Qiu, M., et al. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150124

Collective exerkines mediate physical activity mitigating new-onset heart failure risk in older adults with prediabetes or diabetes: a community-based longitudinal cohort study

Liu, W., Shang, L., Li, P., Yao, Y., Yin, H., Zhang, H., Liu, Z., & Guo, Y. (2026) · Cardiovascular Diabetology · doi:10.1186/s12933-026-03170-8

Skeletal Muscle as an Endocrine Organ

Vincenzo, O. D., Minnetti, M., Poggiogalle, E., Migliaccio, S., & Donini, L. M. (2026) · Endocrinology · doi:10.1007/978-3-030-71067-5_10-1

The Role of Leukemia Inhibitory Factor in Attenuating Skeletal Muscle Atrophy: Mechanisms to Exercise Interventions

Jiang, N., Wang, S., Zhang, J., & Jia, D.-D. (2026) · Cells · doi:10.3390/cells15110981

Erweiterte physiotherapeutische Diagnostik

Bartrow, K. (2026) · Physiotherapie Basics · doi:10.1007/978-3-662-72969-4_14

The local–systemic axis of the skeletal muscle secretome

Ng, S. Y., & Handschin, C. (2026) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2026.07.001

Exercise-responsive crosstalk within local muscle-bone units in osteosarcopenia: from mechanotransduction to secretome signalling

Guan, Z., Fu, X., Zhang, P., Luo, Z., Wu, H., Liu, Q., & Xu, Y. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1923562

Exerkines in Cardiovascular–Kidney–Metabolic Syndrome: An Integrative Framework for Mechanisms and Therapeutic Implications—A Narrative Review

Fan, H., Zhai, C., He, C., Shen, L., Pan, H. Y., & Zheng, W. (2026) · Reviews in Cardiovascular Medicine · doi:10.31083/rcm50762

Molecular drivers of intercellular communication in physical exercise: insights from omics approaches

Pinto, A. C., Corrales, F. J., Domingues, M. R., Ferreira, H. B., Moreira‐Gonçalves, D., Vitorino, R. M. P., Melo, T., & Ferreira, R. M. (2026) · Expert Review of Proteomics · doi:10.1080/14789450.2026.2750126

Disruption of the Muscle–Brain Axis in Ageing: Role of Myokines in Sarcopenia and Neurodegeneration

Molina, V. A. M., Salinas, C. N. L., Vásquez, C. A., Matos, A., & Riofrío, D. A. (2026) · Cells · doi:10.3390/cells15201910

Molecular aspects of the exercise response and training adaptation in skeletal muscle

Furrer, R., & Handschin, C. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.07.026 · Cited by 63 · see citing works

Muscle Mechanics in Metabolic Health and Longevity: The Biochemistry of Training Adaptations

Tabone, M. (2025) · The biochemist · doi:10.3390/biochem5040037 · Cited by 8 · see citing works

Exosomes as Mediators of the Systemic Adaptations to Endurance Exercise

Safdar, A., & Tarnopolsky, M. A. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029827 · Cited by 203 · see citing works

Muscle as a paracrine and endocrine organ

Giudice, J., & Taylor, J. M. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.05.005 · Cited by 331 · see citing works

The local–systemic axis of the skeletal muscle secretome

Ng, S. Y., & Handschin, C. (2026) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2026.07.001