Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

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

Regulation of neuronal survival by the serine-threonine protein kinase Akt

Dudek, H., Datta, S. R., Franke, T. F., Birnbaum, M. J., Yao, R., Cooper, G. M., Segal, R. A., Kaplan, D. R., & Greenberg, M. E. (1997) · Science · doi:10.1126/science.275.5300.661 · Cited by 2,436

Growth Hormone and the Insulin-Like Growth Factor System in Myogenesis*

Florini, J. R., Ewton, D. Z., & Coolican, S. A. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-5-481 · Cited by 1,148

Autonomous Control of Cell and Organ Size by CHICO, a Drosophila Homolog of Vertebrate IRS1–4

Böhni, R., Riesgo‐Escovar, J. R., Oldham, S., Brogiolo, W., Stocker, H., Andruss, B. F., Beckingham, K., & Hafen, E. (1999) · Cell · doi:10.1016/s0092-8674(00)80799-0 · Cited by 840

Drosophila S6 kinase: a regulator of cell size.

Montagne, J., Stewart, M. J., Stocker, H., Hafen, E., Kozma, S., & Thomas, G. (1999) · Science · doi:10.1126/science.285.5436.2126 · Cited by 785

Differentiation Stage-Specific Inhibition of the Raf-MEK-ERK Pathway by Akt

Rommel, C., Clarke, B. A., Zimmermann, S., Nuñez, L., Rossman, R., Reid, K., Moelling, K., Yancopoulos, G. D., & Glass, D. J. (1999) · Science · doi:10.1126/science.286.5445.1738 · Cited by 760

IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1

Musarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652

The Drosophila phosphoinositide 3‐kinase Dp110 promotes cell growth.

Leevers, S. J., Weinkove, D., MacDougall, L. K., Hafen, E., & Waterfield, M. D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01049.x · Cited by 484

Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload

GOLDSPINK, G. (1999) · Journal of Anatomy · doi:10.1046/j.1469-7580.1999.19430323.x · Cited by 435

SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival

Liu, Q., Sasaki, T., Kozieradzki, I., Wakeham, A., Itie, A., Dumont, D. J., & Penninger, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.7.786 · Cited by 341

AMP-activated protein kinase stabilizes FOXO3 in primary myotubes

Sanchez, A. M. J., Candau, R. B., & Bernardi, H. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.176 · Cited by 28

6-Bromoindirubin-3′-oxime intercepts GSK3 signaling to promote and enhance skeletal muscle differentiation affecting miR-206 expression in mice

Ragozzino, E., Brancaccio, M., Costanzo, A. D., Scalabrì, F., Andolfi, G., Wanderlingh, L. G., Patriarca, E. J., Minchiotti, G., Altamura, S., Summa, V., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-54574-4 · Cited by 28

Si-Miao-Yong-An Decoction attenuates isoprenaline-induced myocardial fibrosis in AMPK-driven Akt/mTOR and TGF-β/SMAD3 pathways

Zhao, Y., Sun, D., Chen, Y., Zhan, K., Meng, Q., Zhang, X., Zhu, L., & Yao, X. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110522 · Cited by 28

PTRH2: an adhesion regulated molecular switch at the nexus of life, death, and differentiation

Corpuz, A., Ramos, J. W., & Matter, M. L. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00357-0 · Cited by 28

Role of MicroRNAs and Long Non-Coding RNAs in Sarcopenia

Lee, J., & Kang, H. (2022) · Cells · doi:10.3390/cells11020187 · Cited by 28

Thermal stress affects proliferation and differentiation of turkey satellite cells through the mTOR/S6K pathway in a growth-dependent manner

Xu, J., Strasburg, G. M., Reed, K. M., & Velleman, S. G. (2022) · PLoS ONE · doi:10.1371/journal.pone.0262576 · Cited by 28

Skeletal muscle and metabolic flexibility in response to changing energy demands in wild birds

Swanson, D. L., Zhang, Y., & Jiménez, A. G. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.961392 · Cited by 28

AAV‐Mediated nuclear localized PGC1α4 delivery in muscle ameliorates sarcopenia and aging‐associated metabolic dysfunctions

Guo, M., Zhang, J., Ma, Y., Zhu, Z., Zuo, H., Yao, J., Wu, X., Wang, D., Yu, J., Meng, M., et al. (2023) · Aging Cell · doi:10.1111/acel.13961 · Cited by 28

Therapeutic effects of PEGylated insulin-like growth factor I in the pmn mouse model of motoneuron disease

Jablonka, S., Holtmann, B., Sendtner, M., & Metzger, F. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.09.015 · Cited by 28

Endocrine responses and acute mTOR pathway phosphorylation to resistance exercise with leucine and whey

Lane, M., Herda, T., Fry, A. C., Cooper, M., Andre, M., & Gallagher, P. M. (2017) · Biology of Sport · doi:10.5114/biolsport.2017.65339 · Cited by 28

α−Calcitonin gene-related peptide inhibits autophagy and calpain systems and maintains the stability of neuromuscular junction in denervated muscles

Machado, J., Silveira, W. A., Gonçalves, D. A. P., Schavinski, A. Z., Khan, M. M., Zanon, N. M., Díaz, M. B., Rudolf, R., Kettelhut, Í. D. C., & Navegantes, L. C. C. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.06.024 · Cited by 28

High-intensity interval training-induced hypertrophy in gastrocnemius muscle via improved IGF-I/Akt/FoxO and myostatin/Smad signaling pathways in rats

Biglari, S., Afousi, A. G., Mafi, F., & Shabkhiz, F. (2020) · Physiology International · doi:10.1556/2060.2020.00020 · Cited by 28

Intermittent Reloading Attenuates Muscle Atrophy through Modulating Akt/mTOR Pathway

Miyazaki, M., NOGUCHI, M., & Takemasa, T. (2008) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318163275f · Cited by 28

Calcineurin initiates smooth muscle differentiation in neural crest stem cells

Mann, K. M., Ray, J. L., Moon, E. S., Sass, K. M., & Benson, M. R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200402105 · Cited by 28

Effect of mechanistic/mammalian target of rapamycin complex 1 on mitochondrial dynamics during skeletal muscle hypertrophy

Uemichi, K., Shirai, T., Hanakita, H., & Takemasa, T. (2021) · Physiological Reports · doi:10.14814/phy2.14789 · Cited by 27

Zanthoxylum alkylamides ameliorate protein metabolism in type 2 diabetes mellitus rats by regulating multiple signaling pathways

Wei, X., Yang, B., Chen, X., Wen, L., & Kan, J. (2021) · Food & Function · doi:10.1039/d0fo02695f · Cited by 27

A large-scale transgenic RNAi screen identifies transcription factors that modulate myofiber size in Drosophila

Graça, F. A., Sheffield, N., Puppa, M., Finkelstein, D., Hunt, L. C., & Demontis, F. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009926 · Cited by 27

mTOR activity is essential for retinal pigment epithelium regeneration in zebrafish

Lu, F., Leach, L. L., & Gross, J. M. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1009628 · Cited by 27

Neuromuscular dysfunction in the mutant superoxide dismutase mouse model of amyotrophic lateral sclerosis

Parkhouse, W. S., Cunningham, L., McFee, I. J. L., Miller, J. M., Whitney, D. C., Pelech, S., & Krieger, C. (2008) · Amyotrophic Lateral Sclerosis · doi:10.1080/17482960701725646 · Cited by 27

Functional improvement in mouse models of familial amyotrophic lateral sclerosis by PEGylated insulin-like growth factor I treatment depends on disease severity

Saenger, S., Holtmann, B., Nilges, M. R., Schroeder, S., Hoeflich, A., Kletzl, H., Spooren, W. P. J. M., Ostrowitzki, S., Hanania, T., Sendtner, M., et al. (2012) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482968.2012.679944 · Cited by 27

Analysis of Skeletal Muscle Gene Expression Patterns and the Impact of Functional Capacity in Patients With Systolic Heart Failure

Forman, D. E., Daniels, K. M., Cahalin, L. P., Zavin, A., Allsup, K., Cao, P., Santhanam, M., Joseph, J., Arena, R. A., Lazzari, A. A., et al. (2014) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2014.03.007 · Cited by 27

Effects of Treadmill Exercise on the Recovery of Dopaminergic Neuron Loss and Muscle Atrophy in the 6-OHDA Lesioned Parkinson's Disease Rat Model

Choe, M., Koo, B., An, G. J., & Jeon, S. (2012) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2012.16.5.305 · Cited by 27

Identification of serum biomarkers for aging and anabolic response

Banerjee, C., Ulloor, J., Dillon, E. L., Dahodwala, Q. A., Franklin, B., Storer, T. W., Sebastiani, P., Sheffield‐Moore, M., Urban, R. J., Bhasin, S., et al. (2011) · Immunity & Ageing · doi:10.1186/1742-4933-8-5 · Cited by 27

Functional deficits and insulin-like growth factor-I gene expression following tourniquet-induced injury of skeletal muscle in young and old rats

Hammers, D. W., Merritt, E., Matheny, W., Adamo, M. L., Walters, J., Estep, J. S., & Farrar, R. P. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90418.2008 · Cited by 27

Effects of Dietary Crude Protein Levels and Cysteamine Supplementation on Protein Synthetic and Degradative Signaling in Skeletal Muscle of Finishing Pigs

Zhou, P., Zhang, L., Li, J., Luo, Y., Zhang, B., Xing, S., Zhu, Y., Sun, H., Gao, F., & Zhou, G. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139393 · Cited by 27

Muscle-specific microRNA-206 targets multiple components in dystrophic skeletal muscle representing beneficial adaptations

Amirouche, A., Jahnke, V. E., Lunde, J. A., Koulmann, N., Freyssenet, D. G., & Jasmin, B. J. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00185.2016 · Cited by 27

Melatonin mediates monochromatic green light-induced satellite cell proliferation and muscle growth in chick embryo

Bai, X., Cao, J., Dong, Y., Wang, Z., & Chen, Y. (2019) · PLoS ONE · doi:10.1371/journal.pone.0216392 · Cited by 27

Alterations in IGF-I affect elderly: role of physical activity

Sagiv, M., Chen, Y., Amir, R., & Nir, Y. (2007) · European Review of Aging and Physical Activity · doi:10.1007/s11556-007-0022-1 · Cited by 27

Connexin hemichannels explain the ionic imbalance and lead to atrophy in denervated skeletal muscles

Cisterna, B. A., Vargas, A. A., Puebla, C., & Sáez, J. C. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.020 · Cited by 27

Insulin‐like growth factor‐I E peptides: implications for ageing skeletal muscle

Velloso, C. P., & Harridge, S. D. R. (2009) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2009.00997.x · Cited by 26

Androgen interacts with exercise through the mTOR pathway to induce skeletal muscle hypertrophy

Zeng, F., Zhao, H., & Liao, J. (2017) · Biology of Sport · doi:10.5114/biolsport.2017.69818 · Cited by 26

Lithium Chloride Protects against Sepsis-Induced Skeletal Muscle Atrophy and Cancer Cachexia

Lee, J., Kim, S.-W., Kim, J.-H., Kim, H., Um, J., Jung, D., & Williams, D. R. (2021) · Cells · doi:10.3390/cells10051017 · Cited by 26

Effects of heat stimulation and l -ascorbic acid 2-phosphate supplementation on myogenic differentiation of artificial skeletal muscle tissue constructs

Ikeda, K., Itô, A., Sato, M. S., Kanno, S., Kawabe, Y., & Kamihira, M. (2015) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.2030 · Cited by 26

Naringenin modulates skeletal muscle differentiation via estrogen receptor α and β signal pathway regulation

Pellegrini, M., Bulzomi, P., Galluzzo, P., Lecis, M., Leone, S., Pallottini, V., & Marino, M. (2014) · Genes & Nutrition · doi:10.1007/s12263-014-0425-3 · Cited by 26

Conditional Activation of MET in Differentiated Skeletal Muscle Induces Atrophy

Crepaldi, T., Bersani, F., Scuoppo, C., Accornero, P., Prunotto, C., Taulli, R., Forni, P. E., Leo, C., Chiarle, R., Griffiths, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610916200 · Cited by 26

Identification of Differentially Expressed Genes in Breast Muscle and Skin Fat of Postnatal Pekin Duck

Xu, T., Gu, L., Schachtschneider, K. M., Liu, X., Huang, W., Xie, M., & Hou, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107574 · Cited by 26

Isochlorogenic acid A promotes melanin synthesis in B16 cell through the β-catenin signal pathway

Mamat, N., Dou, J., Lu, X., Eblimit, A., & Akber, A. H. (2017) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx072 · Cited by 26

The factors present in regenerating muscles impact bone marrow-derived mesenchymal stromal/stem cell fusion with myoblasts

Kasprzycka, P., Archacka, K., Kowalski, K., Mierzejewski, B., Zimowska, M., Grabowska, I., Piotrowski, M., Rafałko, M., Ryżko, A., Irhashava, A., et al. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1444-1 · Cited by 26

Emerging Treatment Options for Sarcopenia in Chronic Liver Disease

Kim, Y. (2021) · Life · doi:10.3390/life11030250 · Cited by 26

Point mutated caveolin-3 form (P104L) impairs myoblast differentiation via Akt and p38 signalling reduction, leading to an immature cell signature

Stoppani, E., Rossi, S., Meacci, E., Penna, F., Costelli, P., Bellucci, A., Faggi, F., Maiolo, D., Monti, E., & Fanzani, A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.005 · Cited by 26

Thermal conditions during larval pelagic phase influence subsequent somatic growth of Senegalese sole by modulating gene expression and muscle growth dynamics

Campos, C., Fernandes, J. M. O., Conceição, L. E. C., Engrola, S. A. D., Sousa, V., & Valente, L. M. P. (2013) · Aquaculture · doi:10.1016/j.aquaculture.2013.07.039 · Cited by 26

Indomethacin and ibuprofen preserve gastrocnemius muscle mass in mice bearing the colon‐26 adenocarcinoma

McCarthy, D. O., Whitney, P., Hitt, A., & Al‐Majid, S. (2004) · Research in Nursing & Health · doi:10.1002/nur.20019 · Cited by 26

Calcineurin and skeletal muscle growth

Dunn, S. E., Simard, A. R., Prud'homme, R. A., & Michel, R. N. (2002) · Nature Cell Biology · doi:10.1038/ncb0302-e46a · Cited by 26

Response of Turkey Muscle Satellite Cells to Thermal Challenge. II. Transcriptome Effects in Differentiating Cells

Reed, K. M., Mendoza, K. M., Strasburg, G. M., & Velleman, S. G. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00948 · Cited by 25

Growth Hormone and Insulin-like Growth Factor-I Molecular Weight Isoform Responses to Resistance Exercise Are Sex-Dependent

Pierce, J. R., Martin, B. J., Rarick, K. R., Alemany, J. A., Staab, J. S., Kraemer, W. J., Hymer, W. C., & Nindl, B. C. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00571 · Cited by 25

The androgen receptor in mesenchymal progenitors regulates skeletal muscle mass via Igf1 expression in male mice

Sakai, H., Uno, H., Yamakawa, H., Tanaka, K. Y., Ikedo, A., Uezumi, A., Ohkawa, Y., & Imai, Y. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407768121 · Cited by 25

Elevation of myostatin and FOXOs in prolonged muscular impairment induced by eccentric contractions in rat medial gastrocnemius muscle

Ochi, E., Hirose, T., Hiranuma, K., Min, S.-K., Ishii, N., & Nakazato, K. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00278.2009 · Cited by 25

Individually Tailored Screening of Susceptibility to Sarcopenia Using p53 Codon 72 Polymorphism, Phenotypes, and Conventional Risk Factors

Renzo, L. D., Gratteri, S., Sarlo, F., Cabibbo, A., Colica, C., & LORENZO, A. D. (2014) · Disease Markers · doi:10.1155/2014/743634 · Cited by 25

Black ginseng activates Akt signaling, thereby enhancing myoblast differentiation and myotube growth

Lee, S.-Y., Go, G.-Y., Vuong, T. A., Kim, J. W., Lee, S., Jo, A., An, J. M., Kim, S., Seo, D. W., Kim, J., et al. (2017) · Journal of Ginseng Research · doi:10.1016/j.jgr.2017.08.009 · Cited by 25

Identification of candidate genes and proteins in aging skeletal muscle (sarcopenia) using gene expression and structural analysis

Shafiee, G., Asgari, Y., Soltani, A., Larijani, B. A., & Heshmat, R. (2018) · PeerJ · doi:10.7717/peerj.5239 · Cited by 25

Food deprivation during active phase induces skeletal muscle atrophy via IGF-1 reduction in mice

Abe, T., Kazama, R., Okauchi, H., & Oishi, K. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108160 · Cited by 25

Proteomic analysis of rat laryngeal muscle following denervation

Li, Z.-B., Lehar, M., Samlan, R. A., & Flint, P. W. (2005) · PROTEOMICS · doi:10.1002/pmic.200401329 · Cited by 25

Mechanisms involved in the nutritional regulation of mRNA translation: features of the avian model

Tesseraud, S., Abbas, M., Duchêne, S., Bigot, K., Vaudin, P., & Dupont, J. (2006) · Nutrition Research Reviews · doi:10.1079/nrr2006120 · Cited by 25

IGF-II is up-regulated and myofibres are hypertrophied in regenerating soleus of mice lacking FGF6

Armand, A., Lécolle, S., Launay, T., Pariset, C. C., FIORE, F., Gaspera, B. D., Birnbaum, D., Chanoine, C., & Charbonnier, F. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.02.021 · Cited by 25

GSK3 inhibition improves skeletal muscle function and whole-body metabolism in male mouse models of Duchenne muscular dystrophy

Marcella, B. M., Hockey, B. L., Braun, J. L., Whitley, K. C., Geromella, M. S., Baranowski, R. W., Watson, C. J. F., Silvera, S., Hamstra, S. I., Wasilewicz, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53886-y · Cited by 24

Effects of dietary tryptophan on muscle growth, protein synthesis and antioxidant capacity in hybrid catfish Pelteobagrus vachelli♀ × Leiocassis longirostris♂

Jiang, Q. L., Zhao, Y., Zhou, X., Wu, X., Xu, S.-X., Feng, L., Liu, Y., Jiang, W., Wu, P., Zhao, J., et al. (2021) · British Journal Of Nutrition · doi:10.1017/s0007114521002828 · Cited by 24

A low serum IGF-1 is correlated with sarcopenia in subjects with type 1 diabetes mellitus: Findings from a post-hoc analysis of the iDIAMOND study

Hata, S., Mori, H., Yasuda, T., Irie, Y., Yamamoto, T., Umayahara, Y., Ryomoto, K., Yoshiuchi, K., Yoshida, S., Shimomura, I., et al. (2021) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2021.108998 · Cited by 24

Cellular and molecular modulation of rotator cuff muscle pathophysiology

Fu, C., Huang, A. H., Galatz, L. M., & Han, W. M. (2021) · Journal of Orthopaedic Research® · doi:10.1002/jor.25179 · Cited by 24

Decreased miR-497-5p Suppresses IL-6 Induced Atrophy in Muscle Cells

Freire, P. P., Cury, S. S., Lopes, L. O., Fernández, G. J., Liu, J., de Moraes, L. N., de Oliveira, G., Oliveira, J. S., de Moraes, D., Cabral-Marques, O., et al. (2021) · Cells · doi:10.3390/cells10123527 · Cited by 24

Improving physiological relevance of cell culture: the possibilities, considerations, and future directions of the ex vivo coculture model

Allen, S., Elliott, B., Carson, B. P., & Breen, L. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00473.2022 · Cited by 24

Insulin-Like Growth Factor I (IGF-1) Ec/Mechano Growth Factor – A Splice Variant of IGF-1 within the Growth Plate

Schlegel, W., Raimann, A., Halbauer, D., Scharmer, D., Sagmeister, S., Wessner, B., Helmreich, M., Haeusler, G., & Egerbacher, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076133 · Cited by 24

Exercise-induced signal transduction and gene regulation in skeletal muscle.

Wackerhage, H., & Woods, N. M. (2002) · Europe PMC (PubMed Central) · Cited by 24

Optimization of an in vitro bioassay to monitor growth and formation of myotubes in real time

Murphy, S., Bailey‐Whyte, M., Jakeman, P. M., Kiely, P. A., & Carson, B. P. (2016) · Bioscience Reports · doi:10.1042/bsr20160036 · Cited by 24

Using AAV vectors expressing the β2-adrenoceptor or associated Gα proteins to modulate skeletal muscle mass and muscle fibre size

Hagg, A., Colgan, T. D., Thomson, R. E., Qian, H., Lynch, G. S., & Gregorevic, P. (2016) · Scientific Reports · doi:10.1038/srep23042 · Cited by 24

Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions

Wang, L., Zuo, B., Xu, D., Ren, Z., Zhang, H., Li, X., Lei, M., & Xiong, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040250 · Cited by 24

Featherless and feathered broilers under control versus hot conditions. 2. Breast muscle development and growth in pre- and posthatch periods

Hadad, Y., Cahaner, A., & Halevy, O. (2014) · Poultry Science · doi:10.3382/ps.2013-03592 · Cited by 24

Calcineurin and heat shock protein 72 in functionally overloaded rat plantaris muscle

Oishi, Y., Ogata, T., Ohira, Y., Taniguchi, K., & Roy, R. R. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.049 · Cited by 24

Stem Cells and Plasticity of Skeletal Muscle Cell Differentiation: Potential Application to Cell Therapy for Degenerative Muscular Diseases

Endo, T. (2007) · Regenerative Medicine · doi:10.2217/17460751.2.3.243 · Cited by 24

Urocortin 3 activates AMPK and AKT pathways and enhances glucose disposal in rat skeletal muscle

Roustit, M. M., Vaughan, J. M., Jamieson, P. M., & Cleasby, M. E. (2014) · Journal of Endocrinology · doi:10.1530/joe-14-0181 · Cited by 24

Candidate mechanisms underlying effects of contractile activity on muscle morphology and energetics in cancer cachexia

Khamoui, A. V., & KIM, J. S. (2011) · European Journal of Cancer Care · doi:10.1111/j.1365-2354.2011.01287.x · Cited by 24

Inactivation of muscle insulin and IGF-I receptors and insulin responsiveness

Roith, D. L., Kim, H., Fernandez, A. M., & Accili, D. (2002) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200207000-00004 · Cited by 24

PGF2α-associated vascular smooth muscle hypertrophy is ROS dependent and involves the activation of mTOR, p70S6k, and PTEN

Rice, K. M., Uddemarri, S., Desai, D. H., Morrison, R. G., Harris, R. T., Wright, G. L., & Blough, E. R. (2007) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2007.10.009 · Cited by 24

GSK-3β activity is increased in skeletal muscle after burn injury in rats

Fang, C., Li, B.-G., James, J. H., Yahya, A., Kadeer, N., Guo, X., Xiao, C., Supp, D. M., Kagan, R. J., Hasselgren, P.-O. J., et al. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00244.2007 · Cited by 24

Reconstructing the Regulatory Kinase Pathways of Myogenesis from Phosphopeptide Data

Puente, L. G., Voisin, S. N., Lee, R., & Megeney, L. A. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600134-mcp200 · Cited by 24

Anabolic Activity of a Soy Extract and Three Major Isoflavones in C2C12 Myotubes

Zheng, W., Hemker, M., Xie, M., Soukup, S., & Diel, P. (2018) · Planta Medica · doi:10.1055/a-0598-4812 · Cited by 23

Modified UCN2 peptide treatment improves skeletal muscle mass and function in mouse models of obesity‐induced insulin resistance

Borg, M. L., Massart, J., De Castro Barbosa, T., Archilla‐Ortega, A., Smith, J. A. B., Lanner, J. T., Alsina‐Fernandez, J., Yaden, B., Culver, A. E., Karlsson, H. K. R., et al. (2021) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12746 · Cited by 23

Raptor is critical for increasing the mitochondrial proteome and skeletal muscle force during hypertrophy

Baraldo, M., Nogara, L., Dumitras, A. G., Dondjang, A. H. T., Geremia, A., Scalabrin, M., Türk, C., Tellkamp, F., Zentilin, L., Giacca, M., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202101054rr · Cited by 23

Impaired muscle stem cell function and abnormal myogenesis in acquired myopathies

Deprez, A., Orfi, Z., Rieger, L., & Dumont, N. A. (2022) · Bioscience Reports · doi:10.1042/bsr20220284 · Cited by 23

Protein Turnover in Skeletal Muscle: Looking at Molecular Regulation towards an Active Lifestyle

Ferreira, R. P., & Duarte, J. A. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2044-8277 · Cited by 23

Mechanism of Attenuation of Skeletal Muscle Atrophy by Zinc-α2-Glycoprotein

Russell, S. T., & Tisdale, M. J. (2010) · Endocrinology · doi:10.1210/en.2010-0532 · Cited by 23

TRAF6-mediated regulation of the PI3 kinase (PI3K)–Akt–GSK3β cascade is required for TNF-induced cell survival

Yoon, K., Jung, E. J., & Lee, S. Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.04.007 · Cited by 23

Role of Dystrophin in Airway Smooth Muscle Phenotype, Contraction and Lung Function

Sharma, P. K., Basu, S., Mitchell, R. W., Stelmack, G. L., Anderson, J. E., & Halayko, A. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102737 · Cited by 23

Follistatin could promote the proliferation of duck primary myoblasts by activating PI3K/Akt/mTOR signalling

Li, X., Liu, H., Wang, H., Sun, L., Ding, F., Sun, W., Han, C., & Wang, J. (2014) · Bioscience Reports · doi:10.1042/bsr20140085 · Cited by 23

Insulin involved Akt/ERK and Bcl-2/Bax pathways against oxidative damages in C6 glial cells

Ramalingam, M., & Kim, S.-J. (2014) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2014.970276 · Cited by 23

Treatments for diabetes mellitus type II: New perspectives regarding the possible role of calcium and cAMP interaction

Carvalho, D. S., de Almeida, A. A., Borges, A. F., & Campos, D. V. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.04.002 · Cited by 23

The Mitotic and Metabolic Effects of Phosphatidic Acid in the Primary Muscle Cells of Turbot (Scophthalmus maximus)

Wang, T., Wang, X., Zhou, H., Jiang, H., Mai, K., & He, G. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00221 · Cited by 23

Reversal of age-associated frailty by controlled physical exercise: The pre-clinical and clinical evidences

Arc‐Chagnaud, C., Millán-Domingo, F., Salvador‐Pascual, A., Correas, Á. G., González, G. O., la Rosa, A. D., Carretero, A., Gomez-Cabrera, M. C., & Viña, J. (2019) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2019.08.007 · Cited by 23

Evaluation of an aldo-keto reductase gene signature with prognostic significance in colon cancer via activation of epithelial to mesenchymal transition and the p70S6K pathway

Canlı, S. D., Seza, E. G., Sheraj, I., Gömceli, İ., Turhan, N., Carberry, S., Prehn, J. H. M., Gure, A. O., & Banerjee, S. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa072 · Cited by 23

Early Deconditioning of Human Skeletal Muscles and the Effects of a Thigh Cuff Countermeasure

Fovet, T., Guilhot, C., Stevens, L., Montel, V., Delobel, P., Roumanille, R., Semporé, M.-Y., Freyssenet, D. G., Py, G., Brioche, T., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222112064 · Cited by 23

Innervation of Regenerating Muscle

Slater, C. R., & Schiaffino, S. (2008) · Springer eBooks · doi:10.1007/978-1-4020-6768-6_14 · Cited by 23

Insulin-Like Growth Factor-I-Induced Androgen Receptor Activation Is Mediated by the PI3K/Akt Pathway in C2C12 Skeletal Muscle Cells

Lee, W. J. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0142-8 · Cited by 23

Differential alterations in gene expression profiles contribute to time-dependent effects of nandrolone to prevent denervation atrophy

Qin, W., Pan, J., Bauman, W. A., & Cardozo, C. P. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-596 · Cited by 23

The role of myostatin and bone morphogenetic proteins in muscular disorders

Tsuchida, K. (2006) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.6.2.147 · Cited by 23

Mechanisms of glucocorticoid-induced myopathy

Thissen, J., Schakman, O., & Gilson, H. (2009) · Bone · doi:10.1016/j.bone.2009.07.028 · Cited by 23

Akt-dependent anabolic activity of natural and synthetic brassinosteroids in rat skeletal muscle cells

Esposito, D., Rathinasabapathy, T., Poulev, A., Komarnytsky, S., & Raskin, I. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200028h · Cited by 22

Redox-dependent regulation of satellite cells following aseptic muscle trauma: Implications for sports performance and nutrition

Παπανικολάου, Κ., Veskoukis, A. S., Draganidis, D., Baloyiannis, I., Deli, C. K., Poulios, A., Jamurtas, A. Z., & Fatouros, I. G. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.001 · Cited by 22

Chemotherapy triggers cachexia by deregulating synergetic function of histone‐modifying enzymes

Amrute‐Nayak, M., Pegoli, G., Holler, T., Dávila, A. J. L., Lanzuolo, C., & Nayak, A. (2020) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12645 · Cited by 22

Maslinic acid activates mTORC1 and human TGR5 and induces skeletal muscle hypertrophy

Murata, S., Sasaki, T., Yamauchi, Y., Shimizu, M., & Sato, R. (2021) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbab151 · Cited by 22

Transcriptomic Repositioning Analysis Identifies mTOR Inhibitor as Potential Therapy for Epidermolysis Bullosa Simplex

Lee, G. H., Lekwuttikarn, R., Tafoya, E., Martin, M., Sarin, K. Y., & Teng, J. M. C. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.07.170 · Cited by 22

Critical role of the mTOR pathway in poultry skeletal muscle physiology and meat quality: an opinion paper

Xu, J., & Velleman, S. G. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1228318 · Cited by 22

PI3 Kinase Regulation of Skeletal Muscle Hypertrophy and Atrophy

Glass, D. J. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_78 · Cited by 343

Muscle-specific overexpression of the type 1 IGF receptor results in myoblast-independent muscle hypertrophy via PI3K, and not calcineurin, signaling

Quinn, L. S., Anderson, B. G., & Plymate, S. R. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00160.2007 · Cited by 37

IGF-1 Regulation of Skeletal Muscle Hypertrophy and Atrophy

Glass, D. J. (2009) · Research and perspectives in endocrine interactions · doi:10.1007/978-3-642-04302-4_7 · Cited by 2

IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1

Musarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652

Skeletal muscle hypertrophy is mediated by a Ca2+-dependent calcineurin signalling pathway

Semsarian, C., Wu, M., Ju, Y., Marciniec, T., Yeoh, T., Allen, D. G., Harvey, R. P., & Graham, R. M. (1999) · Nature · doi:10.1038/23054 · Cited by 451