Cited by 475Muscle metabolism and nutritionMuscle Physiology and DisordersMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.

Selective activation of AMPK‐PGC‐1α or PKB‐TSC2‐mTOR signaling can explain specific adaptive responses to endurance or resistance training‐like electrical muscle stimulation

Atherton, Philip J., Babraj, John A., Smith, Kenneth, Singh, Jaipaul, Rennie, Michael J., Wackerhage, Henning·2005·The FASEB Journal

DOI 10.1096/fj.04-2179fje

Open this paper in CoChat — free account

Abstract

Endurance training induces a partial fast-to-slow muscle phenotype transformation and mitochondrial biogenesis but no growth. In contrast, resistance training mainly stimulates muscle protein synthesis resulting in hypertrophy. The aim of this study was to identify signaling events that may mediate the specific adaptations to these types of exercise. Isolated rat muscles were electrically stimulated with either high frequency (HFS; 6x10 repetitions of 3 s-bursts at 100 Hz to mimic resistance training) or low frequency (LFS; 3 h at 10 Hz to mimic endurance training). HFS significantly increased myofibrillar and sarcoplasmic protein synthesis 3 h after stimulation 5.3- and 2.7-fold, respectively. LFS had no significant effect on protein synthesis 3 h after stimulation but increased UCP3 mRNA 11.7-fold, whereas HFS had no significant effect on UCP3 mRNA. Only LFS increased AMPK phosphorylation significantly at Thr172 by approximately 2-fold and increased PGC-1alpha protein to 1.3 times of control. LFS had no effect on PKB phosphorylation but reduced TSC2 phosphorylation at Thr1462 and deactivated translational regulators. In contrast, HFS acutely increased phosphorylation of PKB at Ser473 5.3-fold and the phosphorylation of TSC2, mTOR, GSK-3beta at PKB-sensitive sites. HFS also caused a prolonged activation of the translational regulators p70 S6k, 4E-BP1, eIF-2B, and eEF2. These data suggest that a specific signaling response to LFS is a specific activation of the AMPK-PGC-1alpha signaling pathway which may explain some endurance training adaptations. HFS selectively activates the PKB-TSC2-mTOR cascade causing a prolonged activation of translational regulators, which is consistent with increased protein synthesis and muscle growth. We term this behavior the "AMPK-PKB switch." We hypothesize that the AMPK-PKB switch is a mechanism that partially mediates specific adaptations to endurance and resistance training, respectively.

Integrity signals

Registry

Crossref · 10.1096/fj.04-2179fje

Cites

62 of 62 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
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
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
Mechanism of activation of protein kinase B by insulin and IGF‐1.
Alessi, D. R., Andjelković, M., Caudwell, B., Cron, P. D., MORRICE, N. A., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,014
Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 2,874
Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
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
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911

Flagged first, then by citations

Show all 62 references

Research works printed but not linked: 2

Cheng S. W. Fryer L. G. Carling D. andShepherd P. R.(2004)T2446 is a novel mTOR phosphorylation site regulated by nutrient status.J. Biol. Chem. In press
10.1152/jappl.2001.91.5.1955 · DOI · Paper page

Sorted by citations

Items 101–200 of 473

Mechanisms regulating muscle mass during disuse atrophy and rehabilitation in humans
Marimuthu, K., Murton, A. J., & Greenhaff, P. L. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00962.2010 · Cited by 107
Exercise: the lifelong supplement for healthy ageing and slowing down the onset of frailty
Viña, J., Rodríguez‐Mañas, L., Salvador‐Pascual, A., Tarazona‐Santabalbina, F. J., & Gómez‐Cabrera, M. C. (2016) · The Journal of Physiology · doi:10.1113/jp270536 · Cited by 113
“The AMPK signals for a lower energy state in the cell and inhibits mTOR, telling the cell that protein synthesis should not be activated in endurance exercise (Atherton et al. 2005).”
Background
Obesity: Pathophysiology and Clinical Management
Gurevich-Panigrahi, T., Panigrahi, S., Wiecheć, E., & Łoś, M. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787315568 · Cited by 111
A Ca2+–calmodulin–eEF2K–eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions
Rose, A. J., Alsted, T. J., Jensen, T. E., Kobberø, J. B., Maarbjerg, S., Jensen, J., & Richter, E. A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.167528 · Cited by 106
“…muscle (Williamson et al. 2006b) and there are several lines of evidence that contractions can blunt mRNA translation initiation enzymes via suppression of mTORC1 activity and downstream targets (present study; Atherton et al. 2005; Williamson et al. 2006b; Miranda et al. 2008; Rose et al. 2008).”
BackgroundInfluential
Blunting of adaptive responses to resistance exercise training in women over 75y
Greig, C. A., Gray, C. D., Rankin, D., Young, A., Mann, V., Noble, B., & Atherton, P. J. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.07.010 · Cited by 104
“mRNA transcripts were analyzed according to previously published protocols (Atherton et al. 2005).”
Method
The emerging role of skeletal muscle oxidative metabolism as a biological target and cellular regulator of cancer-induced muscle wasting
Carson, J. A., Hardee, J. P., & VanderVeen, B. N. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.11.005 · Cited by 109
Metabolic and Structural Changes in Lower-Limb Skeletal Muscle Following Neuromuscular Electrical Stimulation: A Systematic Review
Sillen, M. J. H., Franssen, F. M. E., Gosker, H. R., Wouters, E. F. �., & Spruit, M. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069391 · Cited by 108
“increased PKB-TSC2-mTor and protein synthesis) and LF-NMES similar to endurance training (AMPK-PG C1a activation) [31].”
Background
Role of AMP-Activated Protein Kinase in the Molecular Adaptation to Endurance Exercise
Winder, W. W., Taylor, E. B., & Thomson, D. M. (2006) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000233798.62153.50 · Cited by 102
Physical strategies to prevent disuse-induced functional decline in the elderly
Valenzuela, P. L., Morales, J. S., Pareja-Galeano, H., Izquierdo, M., Emanuele, E., de la Villa, P., & Lucia, A. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.07.003 · Cited by 91
The Role of AMP-Activated Protein Kinase in Obesity
Kola, B., Grossman, A. B., & Korbonits, M. (2008) · KARGER eBooks · doi:10.1159/000115366 · Cited by 100
Antagonistic control of muscle cell size by AMPK and mTORC1
Mounier, R., Lantier, L., Leclerc, J., Sotiropoulos, A., Foretz, M., & Viollet, B. (2011) · Cell Cycle · doi:10.4161/cc.10.16.17102 · Cited by 104
Selenium Regulates Cyclooxygenase-2 and Extracellular Signal-Regulated Kinase Signaling Pathways by Activating AMP-Activated Protein Kinase in Colon Cancer Cells
Hwang, J., Kim, Y. M., Surh, Y., Baik, H. W., Lee, S., Ha, J., & Park, O. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1814 · Cited by 100
Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise
Koulmann, N., & Bigard, A. X. (2006) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-0030-9 · Cited by 101
“PCG-1α interacts with nuclear hormone [Ca2+]i PGC-1 AMPK Protein expression MEF2 NFAT MEF2 calcineurin plasma membrane α CaMKIV p38 motor nerve activity metabolic perturbations Dynamics Protein degradation nuclear genome mitochondrial genome Protein expression mitochondriae NRF-1 mtTFA contractile and regulatory prote…”
Influential
Is There a Minimum Intensity Threshold for Resistance Training-Induced Hypertrophic Adaptations?
Schoenfeld, B. J. (2013) · Sports Medicine · doi:10.1007/s40279-013-0088-z · Cited by 97
“pathways that leads to adaptations associated more with endurance than strength [29].”
Background
Transcriptional control of mitochondrial biogenesis and its interface with inflammatory processes
Piantadosi, C. A., & Suliman, H. B. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.01.003 · Cited by 101
Exercise‐induced alterations in extracellular signal‐regulated kinase 1/2 and mammalian target of rapamycin (mTOR) signalling to regulatory mechanisms of mRNA translation in mouse muscle
Williamson, D. L., Kubica, N., Kimball, S. R., & Jefferson, L. S. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103481 · Cited by 96
“Moreover, in isolated muscle preparations, high frequency, but not low frequency, electrical stimulation enhances mTOR signalling and increases protein synthesis (Atherton et al. 2005).”
Background
p-HPEA-EDA, a phenolic compound of virgin olive oil, activates AMP-activated protein kinase to inhibit carcinogenesis
Khanal, P., Oh, W. K., Yun, H. J., Namgoong, G. M., Ahn, S., Kwon, S., Choi, H.-K., & Choi, H. S. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr001 · Cited by 96
Characterization of the equine skeletal muscle transcriptome identifies novel functional responses to exercise training
McGivney, B. A., McGettigan, P., Browne, J. A., Evans, A. C. O., Fonseca, R. G., Loftus, B., Lohan, A. J., MacHugh, D. E., Murphy, B. A., Katz, L. M., et al. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-398 · Cited by 97
“A surprisingly small number of genes were differentially expressed between endurance trained and resistance trained subjects given the very different phenotypic changes and distinct signalling pathways [26,27] associated with each form of exercise.”
Background
Exercise rapidly increases eukaryotic elongation factor 2 phosphorylation in skeletal muscle of men
Rose, A. J., Broholm, C., Kiilerich, K., FINN, S. G., Proud, C. G., Rider, M. H., Richter, E. A., & Kiens, B. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.097154 · Cited by 95
“One study demonstrated that continuous stimulation of isolated rat extensor digitorum longus muscles at 10Hz, but not intermittent stimulation at 100 Hz, increased eEF2 phosphorylation (Atherton et al. 2005).”
BackgroundInfluential
Exercise-induced AMPK activation does not interfere with muscle hypertrophy in response to resistance training in men
Lundberg, T. R., Fernandez-Gonzalo, R., & Tesch, P. A. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01082.2013 · Cited by 91
“Conversely, AE hyperphosphorylated AMPK and increased protein levels of the peroxisome proliferator-activated receptor- coactivator-1 (PGC-1 ) (3).”
Background
Carbon monoxide, skeletal muscle oxidative stress, and mitochondrial biogenesis in humans
Rhodes, M. A., Carraway, M. S., Piantadosi, C. A., Reynolds, C. M., Cherry, A. D., Wester, T. E., Natoli, M. J., Massey, E. W., Moon, R. E., & Suliman, H. B. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00164.2009 · Cited by 91
β-Hydroxy-β-methylbutyrate (HMβ) supplementation stimulates skeletal muscle hypertrophy in rats via the mTOR pathway
Pimentel, G. D., Neto, J. C. R., Lira, F. S., Zanchi, N. E., Ropelle, E. R., Oyama, L. M., do Nascimento, C. M. O., de Mello, M. T., Tufik, S., & dos Santos, R. V. T. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-11 · Cited by 91
Age‐related anabolic resistance after endurance‐type exercise in healthy humans
Durham, W. J., Casperson, S. L., Dillon, E. L., Keske, M. A., Paddon‐Jones, D., Sanford, A. P., Hickner, R. C., Grady, J. J., & Sheffield‐Moore, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150177 · Cited by 93
Aerobic Exercise Alters Skeletal Muscle Molecular Responses to Resistance Exercise
LUNDBERG, T. R., FERNANDEZ-GONZALO, R., GUSTAFSSON, T., & TESCH, P. A. (2012) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318256fbe8 · Cited by 86
“Consequently, it has been put forth that activation of PGC-1> and mTOR signaling pathways are responsible for the specific adaptive responses shown after aerobic and resistance exercise (2).”
Background
Aerobic and resistance training dependent skeletal muscle plasticity in the colon-26 murine model of cancer cachexia.
Khamoui, A. V., Park, B., Kim, D.-H., Yeh, M.-C., Oh, S.-L., Elam, M., Jo, E., Arjmandi, B., Salazar, G., Grant, S., et al. (2016) · Metabolism: Clinical and Experimental · doi:10.1016/j.metabol.2016.01.014 · Cited by 87
“[51] Atherton PJ, Babraj J, Smith K, Singh J, Rennie MJ, Wackerhage H.”
Background
Energy sensing and regulation of gene expression in skeletal muscle
Freyssenet, D. G. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01126.2005 · Cited by 88
“AMPK is activated in skeletal muscle during exercise (25, 107, 158) and electrically stimulated contraction (4, 69, 107, 151).”
Background
Interleukin-6 mediates exercise preconditioning against myocardial ischemia reperfusion injury
McGinnis, G. R., Ballmann, C. G., Peters, B. A., Nanayakkara, G., Roberts, M. D., Amin, R., & Quindry, J. C. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00850.2014 · Cited by 87
Defined Electrical Stimulation Emphasizing Excitability for the Development and Testing of Engineered Skeletal Muscle
Khodabukus, A., & Baar, K. (2011) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2011.0364 · Cited by 84
“47 Second, S6K phosphorylation is normally maximal between 30min and 6 h after resistance exercise 27 or contraction, 47 whereas we measured S6K phosphorylation at 24h. 51 However, all three contraction types can induce skeletal muscle hypertrophy suggesting that different types of muscle…”
The Emerging Role of p53 in Exercise Metabolism
Bartlett, J. D., Close, G. L., Drust, B., & Morton, J. P. (2013) · Sports Medicine · doi:10.1007/s40279-013-0127-9 · Cited by 91
Protein timing and its effects on muscular hypertrophy and strength in individuals engaged in weight-training
Stark, M., Lukaszuk, J. M., Prawitz, A. D., & Salacinski, A. J. (2012) · Journal of the International Society of Sports Nutrition · doi:10.1186/1550-2783-9-54 · Cited by 90
The order of concurrent endurance and resistance exercise modifies mTOR signaling and protein synthesis in rat skeletal muscle
Ogasawara, R., Sato, K., Matsutani, K., Nakazato, K., & Fujita, S. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00647.2013 · Cited by 85
Age-associated decrease in contraction-induced activation of downstream targets of Akt/mTor signaling in skeletal muscle
Funai, K., Parkington, J. D., Carámbula, S. F., & Fielding, R. A. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00277.2005 · Cited by 85
“However, the results of the present study are supported by two studies examining the relation between activation of Akt/mTOR signaling and changes in muscle protein synthesis in vivo (1, 12).”
Electrostimulation during hindlimb unloading modulates PI3K-AKT downstream targets without preventing soleus atrophy and restores slow phenotype through ERK
Dupont, E., Cieniewski‐Bernard, C., Bastide, B., & Stevens, L. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00793.2009 · Cited by 80
Efeito do exercício no sistema imune: resposta, adaptação e sinalização celular
Terra, R., Da-Silva, S. A. G., Salerno, V. P., & Dutra, P. M. L. (2012) · Revista Brasileira de Medicina do Esporte · doi:10.1590/s1517-86922012000300015 · Cited by 84
The impact of immobilisation and inflammation on the regulation of muscle mass and insulin resistance: different routes to similar end‐points
Crossland, H., Skirrow, S., Puthucheary, Z., Constantin‐Teodosiu, D., & Greenhaff, P. L. (2018) · The Journal of Physiology · doi:10.1113/jp275444 · Cited by 84
“…demonstrating that high frequency electrical stimulation of rodent muscle occurs in parallel with increased phosphorylation of these signalling proteins (Atherton et al. 2005) and muscle specific over-expression of Akt in transgenic mice results in muscle hypertrophy (Bodine et al. 2001).”
Background
Cardiac anti‐remodelling effect of aerobic training is associated with a reduction in the calcineurin/NFAT signalling pathway in heart failure mice
Oliveira, R. S. F., Ferreira, J. C. B., Gomes, E. R. D. M., da Paixão, N. A., Rolim, N. P. L., Medeiros, A., Guatimosim, S., & Brum, P. C. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.173948 · Cited by 75
“…skeletal muscle hypertrophy associated with Akt/mTOR signalling activation in high- but not low-intensity exercise training (Nader & Esser, 2001; Atherton et al. 2005), exercise-induced physiological cardiac hypertrophy has been primarily observed in high-intensity exercise training regimens…”
Background
Resistance exercise-induced S6K1 kinase activity is not inhibited in human skeletal muscle despite prior activation of AMPK by high-intensity interval cycling
Apró, W., Moberg, M., Hamilton, D. L., Ekblom, B., van Hall, G., Holmberg, H.-C., & Blomstrand, E. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00486.2014 · Cited by 82
Protein Ingestion Further Augments S6K1 Phosphorylation in Skeletal Muscle Following Resistance Type Exercise in Males
Koopman, R., Pennings, B., Zorenc, A. H. G., & van Loon, L. J. C. (2007) · Journal of Nutrition · doi:10.1093/jn/137.8.1880 · Cited by 76
Heart failure: a model of cardiac and skeletal muscle energetic failure
Mettauer, B., Zoll, J., Garnier, A., & Ventura‐Clapier, R. (2006) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-006-0072-7 · Cited by 77
Enhanced rates of muscle protein synthesis and elevated mTOR signalling following endurance exercise in human subjects: Protein synthesis after aerobic exercise
Mascher, H., Ekblom, B., Rooyackers, O., & Blomstrand, E. (2011) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02274.x · Cited by 71
“The diverse metabolic functions ascribed to AMPK include attenuation of protein synthesis (Atherton et al. 2005, Richter & Ruderman 2009) through inhibition of mTOR phosphorylation via the tuberous sclerosis complex 2 (TSC2).”
Background
Low muscle glycogen concentration does not suppress the anabolic response to resistance exercise
CAMERA, D. M., West, D. W. D., Burd, N. A., Phillips, S. M., GARNHAM, A. P., Hawley, J. A., & Coffey, V. G. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00395.2012 · Cited by 73
Hibernating squirrel muscle activates the endurance exercise pathway despite prolonged immobilization
Xu, R., Andrés‐Mateos, E., Mejı́as, R., MacDonald, E. M., Leinwand, L. A., Merriman, D. K., Fink, R., & Cohn, R. D. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.01.005 · Cited by 69
“The current paradigm suggests that the endurance and resistance pathways are mutually exclusive due to the so-called “AMPK-PKB” switch, which implies that phosphorylated AMPK inhibits the activity of mTOR and its downstream targets (Atherton et al., 2005; Nader, 2006).”
Background
Leucine or carbohydrate supplementation reduces AMPK and eEF2 phosphorylation and extends postprandial muscle protein synthesis in rats
Wilson, G. J., Layman, D. K., Moulton, C. J., Norton, L. E., Anthony, T. G., Proud, C. G., Rupassara, S. I., & Garlick, P. J. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00242.2011 · Cited by 71
Simplified data access on human skeletal muscle transcriptome responses to differentiated exercise
Vissing, K., & Schjerling, P. (2014) · Scientific Data · doi:10.1038/sdata.2014.41 · Cited by 70
Enhanced skeletal muscle ribosome biogenesis, yet attenuated mTORC1 and ribosome biogenesis-related signalling, following short-term concurrent versus single-mode resistance training
Fyfe, J. J., Bishop, D. J., Bartlett, J. D., Hanson, E. D., Anderson, M. J., Garnham, A. P., & Stepto, N. K. (2018) · Scientific Reports · doi:10.1038/s41598-017-18887-6 · Cited by 69
Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise
Burniston, J. G. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.04.007 · Cited by 69
Nutritional strategies to optimize training and racing in middle-distance athletes
Stellingwerff, T., Boit, M. K., & Res, P. T. (2007) · Journal of Sports Sciences · doi:10.1080/02640410701607213 · Cited by 69
“endurance), rather than the nutrition intervention, plays a more dominant role in the divergent signalling pathways and the types of proteins that are synthesized after exercise, which explains the adaptive response and divergent phenotypes (Atherton et al , 2005 ).”
Background
Regulatory mechanisms of skeletal muscle protein turnover during exercise
Rose, A. J., & Richter, E. A. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91375.2008 · Cited by 67
Rapamycin‐insensitive mechanistic target of rapamycin regulates basal and resistance exercise‐induced muscle protein synthesis
Ogasawara, R., & Suginohara, T. (2018) · The FASEB Journal · doi:10.1096/fj.201701422r · Cited by 66
Therapeutic Potential of Mitophagy-Inducing Microflora Metabolite, Urolithin A for Alzheimer’s Disease
Jayatunga, D. P. W., Hone, E., Khaira, H., Lunelli, T., Singh, H., Guillemin, G. J., Fernando, B., Garg, M. L., Verdile, G., & Martins, R. N. (2021) · Nutrients · doi:10.3390/nu13113744 · Cited by 67
“Alternately, the high energy consumption during exercise disrupts the balance between AMP and ATP, leading to AMPK activation followed by induction of PGC-1α [108].”
BackgroundInfluential
Fitness and Lean Mass Increases during Combined Training Independent of Loading Order
Schumann, M., Küüsmaa-Schildt, M., Newton, R. U., SIRPARANTA, A.-I., Syväoja, H., HÄKKINEN, A. H., & Häkkinen, K. (2014) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000000303 · Cited by 75
Inactivation of HDAC5 by SIK1 in AICAR-treated C2C12 Myoblasts
Takemori, H., HASHIMOTO, Y. K., Nakae, J., Olson, E. N., & Okamoto, M. (2009) · Endocrine Journal · doi:10.1507/endocrj.k08e-173 · Cited by 67
Protein Carbonylation and Heat Shock Proteins in Human Skeletal Muscle: Relationships to Age and Sarcopenia
Beltran‐Valls, M. R., Wilkinson, D. J., Narici, M. V., Smith, K., Phillips, B. E., Caporossi, D., & Atherton, P. J. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glu007 · Cited by 69
The Effects of Acute and Chronic Exercise on Skeletal Muscle Proteome
Petriz, B. A., Gomes, C. P. C., de Almeida, J. A., de Oliveira, G. P., Ribeiro, F. M., Pereira, R. W., & Franco, O. L. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25477 · Cited by 72
“Aerobic training is shown to regulate the AMPK-TSC2 molecules, inhibiting protein synthesis through the downregulation of mTOR (Atherton et al., 2005), while strength training activates the PI3K-Akt-mTOR pathway, leading to proteins synthesis and muscle growth (Coffey and Hawley, 2007).”
BackgroundInfluential
Musclin, A Myokine Induced by Aerobic Exercise, Retards Muscle Atrophy During Cancer Cachexia in Mice
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
“In the former, activation of the Ser/Thr kinase AKT enhances protein synthesis [9], ultimately causing hypertrophy especially of glycolytic fibers (type II fibers) [10].”
Background
Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type
Rose, A. J., Bisiani, B., Vistisen, B., Kiens, B., & Richter, E. A. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90806.2008 · Cited by 66
PGC-1 isoforms and their target genes are expressed differently in human skeletal muscle following resistance and endurance exercise
Silvennoinen, M., Ahtiainen, J. P., Hulmi, J. J., Pekkala, S., Taipale, R. S., Nindl, B. C., Laine, T., Häkkinen, K., Selänne, H., Kyröläinen, H., et al. (2015) · Physiological Reports · doi:10.14814/phy2.12563 · Cited by 66
“Yet, there have been attempts to identify single signaling cascades or molecules that could work as a master regulator for controlling exercise-specific adaptations (Atherton et al. 2005; Baar and Esser 1999).”
Background
Role of Akt2 in contraction-stimulated cell signaling and glucose uptake in skeletal muscle
Sakamoto, K., Arnolds, D. E., Fujii, N., Kramer, H. F., Hirshman, M. F., & Goodyear, L. J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00204.2006 · Cited by 63
“Although early studies suggested that Akt was not activated by either contraction (2, 25, 39) or physical exercise (26, 46, 48), more recent data from our laboratory and those of others have convincingly shown that Akt is activated by exercise and contraction in both rodent (3, 28, 30, 34, 36) and human skeletal muscl…”
Result
Optimizing Intramuscular Adaptations to Aerobic Exercise: Effects of Carbohydrate Restriction and Protein Supplementation on Mitochondrial Biogenesis
Margolis, L. M., & Pasiakos, S. M. (2013) · Advances in Nutrition · doi:10.3945/an.113.004572 · Cited by 63
“The metabolic demand associated with sustained aerobic exercise increases AMPK phosphorylation, which appears to be an upstream intracellular regulator of PGC-1a activity (43,44), because AMPK directly phosphorylates PGC1a (45).”
Background
Improvement of obesity-linked skeletal muscle insulin resistance by strength and endurance training
Meo, S. D., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-17-0186 · Cited by 69
“…simulating strength and endurance training in isolated rat extensor digitorum longus and soleus muscles, showed selective activation of the Akt-mTOR signaling cascade with the strength and preferential activation of AMPK-PGC-1 α signaling with the endurance protocol (Atherton et al. 2005).”
Background
Electrical pulse stimulation: an in vitro exercise model for the induction of human skeletal muscle cell hypertrophy. A proof‐of‐concept study
Tarum, J., Folkesson, M., Atherton, P. J., & Kadi, F. (2017) · Experimental Physiology · doi:10.1113/ep086581 · Cited by 68
“Thus, the selective activation of these two molecular sensors contributes to divergent adaptations occurring in human skeletal muscle in response to strength and endurance activities (Atherton et al. 2005).”
Background
Effects of Traditional and Vascular Restricted Strength Training Program With Equalized Volume on Isometric and Dynamic Strength, Muscle Thickness, Electromyographic Activity, and Endothelial Function Adaptations in Young Adults
Ramis, T. R., Muller, C. H. D. L., Boeno, F. P., Teixeira, B. C., Rech, A., Pompermayer, M. G., Medeiros, N. D. S., Reischak-Oliveira, Á., Pinto, R. S., & Ribeiro, J. L. (2018) · The Journal of Strength and Conditioning Research · doi:10.1519/jsc.0000000000002717 · Cited by 63
“The Akt promotes the activation of mTOR and GSK-3B (glycogen synthase kinase-3B) both inducing skeletal muscle hypertrophy (4).”
Background
Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities
Mesquita, P. H. C., Vann, C. G., Phillips, S. M., McKendry, J., Young, K. C., Kavazis, A. N., & Roberts, M. D. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.725866 · Cited by 62
Low‐Frequency Electroacupuncture Improves Insulin Sensitivity in Obese Diabetic Mice through Activation of SIRT1/PGC‐1α in Skeletal Muscle
Liang, F.-X., Chen, R., Nakagawa, A., Nishizawa, M., Tsuda, S., Wang, H., & Koya, D. (2010) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2011/735297 · Cited by 62
“These results indicated that EA offers a beneficial effect on insulin resistance in obese and diabetic db/db mice, at least partly, via stimulation of SIRT1/PGC-1α, thus resulting in improved insulin signal.”
Background
Molecular Adaptations to Concurrent Training
de Souza, E., Tricoli, V., Roschel, H., Brum, P. C., Bacurau, A. V. N., Ferreira, J. C. B., Aoki, M. S., Neves, M., Aihara, A. Y., Fernandes, A. D. R. C., et al. (2012) · International Journal of Sports Medicine · doi:10.1055/s-0032-1312627 · Cited by 68
“This hypothesis suggests that CT may simultaneously activate competing intracellular pathways, resulting in interference between the strength and endurance training-induced adaptations [ 2 , 8 , 32 ] . post-test when compared to C (CT = 6.1 ± 0.58 %; IT = 8.3 ± 0.88 %; ST = 3.2 ± 0.66 %).”
BackgroundInfluential
The Rationale for Consuming Protein Blends in Sports Nutrition
Paul, G. L. (2009) · Journal of the American College of Nutrition · doi:10.1080/07315724.2009.10718113 · Cited by 60
Exercise- and nutrient-controlled mechanisms involved in maintenance of the musculoskeletal mass
Rennie, M. J. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351302 · Cited by 60
Akt/protein kinase B in skeletal muscle physiology and pathology
Wu, M., Falasca, M., & Blough, E. R. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22353 · Cited by 60
“Similarly, Akt is rapidly activated by muscle contraction suggesting that it may play a role in contraction-induced muscle glucose uptake and protein synthesis (Atherton et al., 2005; Bruss et al., 2005; Arias et al., 2007; Katta et al., 2009b; Wu et al., 2009b).”
BackgroundInfluential
Tea catechin ingestion combined with habitual exercise suppresses the aging-associated decline in physical performance in senescence-accelerated mice
Murase, T., Haramizu, S., Ota, N., & Hase, T. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00880.2007 · Cited by 59
Lipid-induced mTOR activation in rat skeletal muscle reversed by exercise and 5′-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside
Rivas, D. A., Yaspelkis, B. B., Hawley, J. A., & Lessard, S. J. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0202 · Cited by 60
“Opposing roles for these two training modes on mTOR activation are not surprising given the highly contrasting nature of muscle adaptations resulting from endurance and resistance exercise (Atherton et al. 2005, Coffey & Hawley 2007).”
Influential
Ferulic acid regulates muscle fiber type formation through the Sirt1/AMPK signaling pathway
Chen, X., Guo, Y., Jia, G., Zhao, H. Y., Liu, G., & Huang, Z. (2018) · Food & Function · doi:10.1039/c8fo01902a · Cited by 60
Akt1-Mediated Fast/Glycolytic Skeletal Muscle Growth Attenuates Renal Damage in Experimental Kidney Disease
Hanatani, S., Izumiya, Y., Araki, S., Rokutanda, T., Kimura, Y., Walsh, K., & Ogawa, H. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013091025 · Cited by 58
Cyclic stretch reduces myofibrillar protein synthesis despite increases in FAK and anabolic signalling in L6 cells
Atherton, P. J., Szewczyk, N. J., Selby, A., Rankin, D., Hillier, K., Smith, K., Rennie, M. J., & Loughna, P. T. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.169854 · Cited by 58
“After exercise, the rebound of MPS is associated with upregulated anabolic signalling through the classic ‘anabolic’ signalling cascade (PKB/Akt–mTORC1) (Atherton et al. 2005; Kumar et al. 2009a).”
Background
Downhill Running Excessive Training Inhibits Hypertrophy in Mice Skeletal Muscles with Different Fiber Type Composition
da Rocha, A. L., Pereira, B. C., Pauli, J. R., de Souza, C. T., Teixeira, G. R., Lira, F. S., Cintra, D. E., Ropelle, E. R., Júnior, C. R. B., & da Silva, A. S. R. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25197 · Cited by 58
“In accordance, Atherton et al. (2005) showed that lowfrequency stimulation had no effect on pAkt, but reduced pTSC2 (Thr1462) in mixed EDL and soleus samples.”
Background
Chikusetsu Saponin IVa Ameliorates Cerebral Ischemia Reperfusion Injury in Diabetic Mice via Adiponectin-Mediated AMPK/GSK-3β Pathway In Vivo and In Vitro
Duan, J., Yin, Y., Cui, J., Yan, J., Zhu, Y., Guan, Y., Wei, G., Weng, Y., Wu, X., Guo, C., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9033-x · Cited by 57
Intracellular signalling pathways regulating the adaptation of skeletal muscle to exercise and nutritional changes.
Matsakas, A., & Patel, K. (2009) · PubMed · doi:10.14670/hh-24.209 · Cited by 57
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 68
The effect of concurrent training organisation in youth elite soccer players
Enright, K. J., Morton, J. P., Iga, J., & Drust, B. (2015) · European Journal of Applied Physiology · doi:10.1007/s00421-015-3218-5 · Cited by 57
“…training intensities (Docherty and Sporer, 2000), an incompatible hormonal (Bell et al., 2000) and (or) molecular signalling environment (Atherton et al., 2005) the ‘sequence’ or ‘order’ of training (Chtaha et al., 2008), the recovery time between training bouts (Craig et al., 1991) and…”
Background
The role of the neural stimulus in regulating skeletal muscle hypertrophy
Alix‐Fages, C., Vecchio, A. D., Baz-Valle, E., Santos‐Concejero, J., & Balsalobre‐Fernández, C. (2022) · European Journal of Applied Physiology · doi:10.1007/s00421-022-04906-6 · Cited by 54
Resistance Training to Momentary Muscular Failure Improves Cardiovascular Fitness in Humans: A Review of Acute Physiological Responses and Chronic Physiological Adaptations
Steele, J., Fisher, J. P., McGuff, D., Bruce‐Low, S., & Smith, D. (2012) · Solent University Research Portal (Solent University) · Cited by 52
Alcohol Regulates Eukaryotic Elongation Factor 2 Phosphorylation via an AMP-activated Protein Kinase-dependent Mechanism in C2C12 Skeletal Myocytes
Hong‐Brown, L. Q., Brown, C. R., Huber, D. S., & Lang, C. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606593200 · Cited by 53
Mammalian target of rapamycin-independent S6K1 and 4E-BP1 phosphorylation during contraction in rat skeletal muscle
Liu, Y., Vertommen, D., Rider, M. H., & Lai, Y. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.005 · Cited by 53
Akt1–Mediated Skeletal Muscle Growth Attenuates Cardiac Dysfunction and Remodeling After Experimental Myocardial Infarction
Araki, S., Izumiya, Y., Hanatani, S., Rokutanda, T., Usuku, H., Akasaki, Y., Takeo, T., Nakagata, N., Walsh, K. X., & Ogawa, H. (2011) · Circulation Heart Failure · doi:10.1161/circheartfailure.111.964783 · Cited by 53
Cachectic skeletal muscle response to a novel bout of low-frequency stimulation
Puppa, M., Murphy, E. A., Fayad, R., Hand, G. A., & Carson, J. A. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01270.2013 · Cited by 52
“Contraction-induced activation of AMPK is associated with increased PGC-1 protein expression (2).”
Diet, energy metabolism and mitochondrial biogenesis
Civitarese, A. E., Smith, S. R., & Ravussin, É. (2007) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3282f0ecd2 · Cited by 52
Effects of Elevated Circulating Hormones on Resistance Exercise-Induced Akt Signaling
Spiering, B. A., Kraemer, W. J., Anderson, J. M., Armstrong, L. E., Nindl, B. C., Volek, J. S., Judelson, D. A., JOSEPH, M., Vingren, J. L., Hatfield, D. L., et al. (2008) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31816722bd · Cited by 52
Fiber hypertrophy and increased oxidative capacity can occur simultaneously in pig glycolytic skeletal muscle
Scheffler, T. L., Scheffler, J. M., Park, S., Kasten, S., Wu, Y., McMillan, R. P., Hulver, M. W., Frisard, M. I., & Gerrard, D. E. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00002.2013 · Cited by 51
The effect of two concurrent exercise modalities on serum concentrations of FGF21, irisin, follistatin, and myostatin in men with type 2 diabetes mellitus
Rad, M. M., Bijeh, N., Hosseini, S. R. A., & Saeb, A. R. (2020) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2020.1829649 · Cited by 51
How nutrition and exercise maintain the human musculoskeletal mass
Wackerhage, H., & Rennie, M. J. (2006) · Journal of Anatomy · doi:10.1111/j.1469-7580.2006.00544.x · Cited by 52
“Also, the selective activation of AMPK by endurance training-like interventions and activation of PKB-TSC2-mTOR signalling by resistance training-like interventions might explain the specific adaptations to these types of exercise in rodent muscle (Atherton et al. 2005).”
Background
Actuality of Warburg’s views in our understanding of renal cancer metabolism
Godinot, C., de Laplanche, E., Hervouet, É., & Simonnet, H. (2007) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-007-9088-8 · Cited by 49
“Indeed NRFs and PGC-1 family co-activators control mitochondrial biogenesis, likely via the AMP kinase that activates their expression in response to low ATP ( Atherton et al. 2005 ).”
Background
Skeletal muscle mitochondrial volume and myozenin-1 protein differences exist between high versus low anabolic responders to resistance training
Roberts, M. D., Romero, M. A., Mobley, C. B., Mumford, P. W., Roberson, P. A., Haun, C. T., Vann, C. G., Osburn, S. C., Holmes, H. H., Greer, R. A., et al. (2018) · PeerJ · doi:10.7717/peerj.5338 · Cited by 51
“…or greater mitochondrial involvement with muscle hypertrophy in HI responders is seemingly paradoxical given that the intramuscular signaling mechanisms which facilitate muscle protein accretion with RET and mitochondrial biogenesis with endurance training are dichotomous (Atherton et al., 2005).”
Background
Blood flow restricted resistance exercise and reductions in oxygen tension attenuate mitochondrial H2O2 emission rates in human skeletal muscle
Petrick, H. L., Pignanelli, C., Barbeau, P., Churchward‐Venne, T. A., Dennis, K. M. J. H., van Loon, L. J. C., Burr, J. F., Goossens, G. H., & Holloway, G. P. (2019) · The Journal of Physiology · doi:10.1113/jp277765 · Cited by 54
“However, because AMPK is capable of inhibiting anabolic pathways (Hawley, 2009), acute RE is suggested to be a less potent activator of AMPK compared to aerobic exercise (Atherton et al. 2005; Lundberg et al. 2014), and recent evidence suggests that a greater increase in AMPK phosphorylation is not present following B…”
Background
Exercise-Regulated Mitochondrial and Nuclear Signalling Networks in Skeletal Muscle
Reisman, E. G., Hawley, J. A., & Hoffman, N. J. (2024) · Sports Medicine · doi:10.1007/s40279-024-02007-2 · Cited by 57
Changes in structural and metabolic muscle characteristics following exercise-based interventions in patients with COPD: a systematic review
Brandt, J. D., Spruit, M. A., Derave, W., Hansen, D., Vanfleteren, L. E. G. W., & Burtin, C. (2016) · Expert Review of Respiratory Medicine · doi:10.1586/17476348.2016.1157472 · Cited by 48
“resistance training and LF-NMES comparable to aerobic training [62,63].”
Background
Omega-3 Fatty Acids-Enriched Fish Oil Activates AMPK/PGC-1α Signaling and Prevents Obesity-Related Skeletal Muscle Wasting
Liu, S., Chiu, C., Wang, L.-P., & Chiang, M. (2019) · Marine Drugs · doi:10.3390/md17060380 · Cited by 49
“Moreover, Atherton et al. (2005) indicate that the inhibition of AMPK/mTOR signaling pathway (i.e., the inhibition of phosphorylated AMPK) would lead to the inhibition of protein synthesis and lack of hypertrophic muscles [36].”
Background
Truncated splice variant PGC-1α4 is not associated with exercise-induced human muscle hypertrophy
Lundberg, T. R., Fernandez‐Gonzalo, R., Norrbom, J., Fischer, H., Tesch, P. A., & Gustafsson, T. P. (2014) · Acta Physiologica · doi:10.1111/apha.12310 · Cited by 46
“Over time, several molecular ‘master regulators’ have been purported to control exercise-specific adaptations (Baar & Esser 1999, Nader & Esser 2001, Atherton et al. 2005, Terzis et al. 2008).”
Background
Kinase-specific responsiveness to incremental contractile activity in skeletal muscle with low and high mitochondrial content
Ljubicic, V., & Hood, D. A. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90276.2008 · Cited by 46
Effects of divergent resistance exercise contraction mode and dietary supplementation type on anabolic signalling, muscle protein synthesis and muscle hypertrophy
Rahbek, S. K., Farup, J., Møller, A. B., Vendelbo, M. H., Holm, L., Jessen, N., & Vissing, K. (2014) · Amino Acids · doi:10.1007/s00726-014-1792-1 · Cited by 46
Dihydromyricetin Improves Physical Performance under Simulated High Altitude
Zou, D., Chen, K., Liu, P., Chang, H., Zhu, J., & Mi, M. (2014) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000000336 · Cited by 46
Flavonoids modulate AMPK/PGC-1α and interconnected pathways toward potential neuroprotective activities
Gravandi, M. M., Fakhri, S., Zarneshan, S. N., Yarmohammadi, A., & Khan, H. Z. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00750-3 · Cited by 45

Authors: Atherton, P. J., Babraj, J. A., Smith, K., Singh, J., Rennie, M. J., & Wackerhage, H.
Affiliations: University of Nottingham (GB)
University of Dundee (GB)
University of Lancashire (GB)
ORCID: Atherton, Philip J.
Babraj, John A.
Smith, Kenneth
Singh, Jaipaul
Rennie, Michael J.
Wackerhage, Henning
Venue: The FASEB Journal
Publisher: Wiley
Published: 2005-02-16
Volume: 19
Issue: 7
Pages: 1-23
ISSN: 0892-6638 (ISSN-L)
1530-6860
DOI: 10.1096/fj.04-2179fje
OpenAlex: W2115928938
Cited by: 475
References: 62
Citations by year: 2026: 9 · 2025: 11 · 2024: 10 · 2023: 21 · 2022: 15 · 2021: 15 · 2020: 18 · 2019: 25 · 2018: 35 · 2017: 16 · 2016: 22 · 2015: 20 · 2014: 30 · 2013: 33 · 2012: 23
FWCI: 12.47
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The FASEB Journal (publishedVersion)
PubMed (publishedVersion)
CLOK (University of Central Lancashire) (submittedVersion)
Funders: National Institutes of Health (AR 49869)
Biotechnology and Biological Sciences Research Council
Diabetes UK
Tenovus
University of Central Lancashire
University of Dundee
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: AMPK/PGC-1α signaling, neuromuscular electrical stimulation, high-frequency stimulation, low-frequency stimulation, endurance training adaptation, resistance training adaptation, muscle protein synthesis, muscle hypertrophy, mitochondrial biogenesis, UCP3, translational regulation, p70S6K, 4E-BP1
MeSH terms: Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Tuberous Sclerosis Complex 2 Protein, Adaptation, Physiological, Adenylate Kinase, Animals, Electric Stimulation, Enzyme Activation, Physical Exertion, Male, Muscle Contraction, Muscle Proteins, Myofibrils, Phosphorylation, Physical Conditioning, Animal, Physical Endurance, Protein Kinases, Sarcoplasmic Reticulum, Transcription Factors, Signal Transduction, RNA-Binding Proteins, Rats, Wistar, Muscle, Skeletal, Mitogen-Activated Protein Kinases, Tumor Suppressor Proteins, Proto-Oncogene Proteins c-akt, Rats, TOR Serine-Threonine Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Selective activation of AMPK‐PGC‐1α or PKB‐TSC2‐mTOR signaling can explain specific adaptive responses to endurance or resistance training‐like electrical muscle stimulation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks