Signaling pathways weigh in on decisions to make or break skeletal muscle

TGF-β SIGNAL TRANSDUCTION

Massagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571

THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

Baldwin, A. S. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.649 · Cited by 5,882

Phosphorylation meets ubiquitination: the control of NF-κB activity

Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766

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 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

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

Double muscling in cattle due to mutations in the myostatin gene

McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039

Signal transduction by tumor necrosis factor and its relatives.

Baud, V., & Karin, M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02064-5 · Cited by 1,741

The intersection between aging and cardiovascular disease

North, B. J., & Sinclair, D. A. (2012) · Circulation Research · doi:10.1161/circresaha.111.246876 · Cited by 1,585

Skeletal muscle wasting in cachexia and sarcopenia: molecular pathophysiology and impact of exercise training

Lenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 498

Nuclear factor-kappa B signaling in skeletal muscle atrophy

Li, H., Malhotra, S., & Kumar, A. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0373-8 · Cited by 464

The p38 MAPK signaling pathway: A major regulator of skeletal muscle development

Keren, A., Tamir, Y., & Bengal, E. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.03.017 · Cited by 372

Diagnostic and Therapeutic Challenges in Patients With Coexistent Chronic Obstructive Pulmonary Disease and Chronic Heart Failure

Jemtel, T. H. L., Padeletti, M., & Jelić, S. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2006.08.046 · Cited by 321

Models of accelerated sarcopenia: critical pieces for solving the puzzle of age-related muscle atrophy

Buford, T. W., Anton, S. D., Judge, A. R., Marzetti, E., Wohlgemuth, S. E., Carter, C. S., Leeuwenburgh, C., Pahor, M., & Manini, T. M. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.04.004 · Cited by 295

Cancer cachexia—pathophysiology and management

Suzuki, H., Asakawa, A., Amitani, H., Nakamura, N., & Inui, A. (2013) · Journal of Gastroenterology · doi:10.1007/s00535-013-0787-0 · Cited by 285

NF-κB Regulation of YY1 Inhibits Skeletal Myogenesis through Transcriptional Silencing of Myofibrillar Genes

Wang, H., Hertlein, E. K., Bakkar, N., Sun, H., Acharyya, S., Wang, J., Carathers, M., Davuluri, R. V., & D, D. C. G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02020-06 · Cited by 259

NF-κB Signaling: A Tale of Two Pathways in Skeletal Myogenesis

Bakkar, N., & Guttridge, D. C. (2010) · Physiological Reviews · doi:10.1152/physrev.00040.2009 · Cited by 203

Atrogin-1/MAFbx and MuRF1 are downregulated in aging-related loss of skeletal muscle

Edstrom, E., Altun, M., Hagglund, M., & Ulfhake, B. (2006) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/61.7.663 · Cited by 196

Palmitate increases superoxide production through mitochondrial electron transport chain and NADPH oxidase activity in skeletal muscle cells

Lambertucci, R. H., Hirabara, S. M., Silveira, L. R., Levada‐Pires, A. C., Curi, R., & Pithon‐Curi, T. C. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21463 · Cited by 188

Diabetes, Sarcopenia, and Frailty

Morley, J. E. (2008) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2008.03.004 · Cited by 186

Skeletal muscle and nuclear hormone receptors: Implications for cardiovascular and metabolic disease

Smith, A. G., & Muscat, G. E. O. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.03.002 · Cited by 182

The effect of relaxin on the musculoskeletal system

Dehghan, F., Haerian, B. S., Muniandy, S., Yusof, A., Dragoo, J. L., & Salleh, N. (2013) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.12149 · Cited by 180

Type 2 diabetes is associated with low muscle mass in older adults

Kim, K., Park, K., Kim, M., Kim, S., Cho, Y., & Park, S. W. (2014) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.12189 · Cited by 184

Phytoecdysteroids increase protein synthesis in skeletal muscle cells.

Gorelick-Feldman, J., MacLean, D., Ilic, N., Poulev, A., Lila, M. A., Cheng, D., & Raskin, I. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf073059z · Cited by 166

Differences in Muscle Protein Synthesis and Anabolic Signaling in the Postabsorptive State and in Response to Food in 65–80 Year Old Men and Women

Smith, G. I., Atherton, P., Villareal, D. T., Frimel, T. N., Rankin, D., Rennie, M. J., & Mittendorfer, B. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001875 · Cited by 168

Modifying muscle mass – the endocrine perspective

Solomon, A. M., & Bouloux, P. M. G. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06837 · Cited by 156

Aging-sensitive cellular and molecular mechanisms associated with skeletal muscle hypertrophy

Haddad, F., & Adams, G. R. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01227.2005 · Cited by 158

Proteome Dynamics during C2C12 Myoblast Differentiation

Kislinger, T., Gramolini, A. O., Pan, Y., Rahman, K., MacLennan, D. H., & Emili, A. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400182-mcp200 · Cited by 152

TNF Inhibits Notch-1 in Skeletal Muscle Cells by Ezh2 and DNA Methylation Mediated Repression: Implications in Duchenne Muscular Dystrophy

Acharyya, S., Sharma, S. M., Cheng, A. S. L., Ladner, K. J., He, W. A., Kline, W. O., Wang, H., Ostrowski, M. C., Huang, T. H. ‐., & Guttridge, D. C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012479 · Cited by 140

Epigallocathechin-3 gallate inhibits cardiac hypertrophy through blocking reactive oxidative species-dependent and -independent signal pathways

Li, H., Huang, Y., Zhang, C.-N., Liu, G., Wei, Y.-S., Wang, A.-B., Liu, Y.-Q., Hui, R.-T., Wei, C., Williams, G. M., et al. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.005 · Cited by 136

Parallel protein and transcript profiles of FSHD patient muscles correlate to the D4Z4 arrangement and reveal a common impairment of slow to fast fibre differentiation and a general deregulation of MyoD‐dependent genes

Celegato, B., Capitanio, D., Pescatori, M., Romualdi, C., Pacchioni, B., Cagnin, S., Viganò, A., Colantoni, L., Begum, S., Ricci, E., et al. (2006) · PROTEOMICS · doi:10.1002/pmic.200600056 · Cited by 141

Polyphenols in the treatment of inflammatory bowel disease and acute pancreatitis

Shapiro, H., Singer, P., Halpern, Z., & Bruck, R. (2006) · Gut · doi:10.1136/gut.2006.094599 · Cited by 130

The Impact of Aging on Cardio and Cerebrovascular Diseases

Izzo, C., Carrizzo, A., Alfano, A., Virtuoso, N., Capunzo, M., Calabrese, M., Simone, E. D., Sciarretta, S., Frati, G., Oliveti, M., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020481 · Cited by 134

Cancer Cachexia Signaling Pathways Continue to Emerge Yet Much Still Points to the Proteasome

Acharyya, S., & Guttridge, D. C. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2307 · Cited by 127

Diabetes and Frailty: Two Converging Conditions?

Sinclair, A. J., & Rodríguez‐Mañas, L. (2015) · Canadian Journal of Diabetes · doi:10.1016/j.jcjd.2015.09.004 · Cited by 124

Effects of Amino Acids Supplement on Physiological Adaptations to Resistance Training

Kraemer, W. J., Hatfield, D. L., Volek, J. S., Fragala, M. S., Vingren, J. L., Anderson, J. M., Spiering, B. A., Thomas, G. A., Ho, J., Quann, E. E., et al. (2009) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318194cc75 · Cited by 109

Age-dependent increase in oxidative stress in gastrocnemius muscle with unloading

Siu, P. M., Pistilli, E. E., & Alway, S. E. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90800.2008 · Cited by 105

Sexually dimorphic effect of aging on skeletal muscle protein synthesis

Smith, G. I., Reeds, D. N., Hall, A. M., Chambers, K. T., Finck, B. N., & Mittendorfer, B. (2012) · Biology of Sex Differences · doi:10.1186/2042-6410-3-11 · Cited by 105

Obesity and diabetes as accelerators of functional decline: Can lifestyle interventions maintain functional status in high risk older adults?

Anton, S. D., Karabetian, C., Naugle, K., & Buford, T. W. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.06.007 · Cited by 100

METTL21C Is a Potential Pleiotropic Gene for Osteoporosis and Sarcopenia Acting Through the Modulation of the NF-κB Signaling Pathway

Huang, J. M., Hsu, Y., Mo, C., de Abreu, E. L., Kiel, D. P., Bonewald, L. F., Brotto, M., & Karasik, D. (2014) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2200 · Cited by 99

Skeletal muscle mitochondrial uncoupling in a murine cancer cachexia model

Tzika, A. A., de Oliveira, C. C. F., Shestov, A. A., Constantinou, C., Psychogios, N., Righi, V., Mintzopoulos, D., Busquets, S., López-Soriano, F. J., Milot, S. M., et al. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1998 · Cited by 96

Skeletal muscle cytokines: regulation by pathogen-associated molecules and catabolic hormones

Frost, R. A., & Lang, C. H. (2005) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000165003.16578.2d · Cited by 94

Molecular signaling pathways regulating muscle proteolysis during atrophy

Franch, H. A., & Price, S. R. (2005) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000165005.01331.45 · Cited by 94

Molecular profiles of Quadriceps muscle in myostatin-null mice reveal PI3K and apoptotic pathways as myostatin targets

Chelh, I., Meunier, B., Picard, B. B., Reecy, M. J., Chevalier, C., Hocquette, J.-F. J.-F., & Cassar‐Malek, I. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-196 · Cited by 89

Sepsis increases the expression and activity of the transcription factor Forkhead Box O 1 (FOXO1) in skeletal muscle by a glucocorticoid-dependent mechanism

Smith, I. J., Alamdari, N., O’Neal, P., GONNELLA, P. A., Aversa, Z., & Hasselgren, P.-O. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.01.006 · Cited by 88

Combined isometric, concentric, and eccentric resistance exercise prevents unloading-induced muscle atrophy in rats

Adams, G. R., Haddad, F., Bodell, P. W., Tran, P. D., & Baldwin, K. M. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00669.2007 · Cited by 88

In vivo Phosphoproteome of Human Skeletal Muscle Revealed by Phosphopeptide Enrichment and HPLC−ESI−MS/MS

Højlund, K., Bowen, B. P., Hwang, H., Flynn, C. R., Madireddy, L., Geetha, T., Langlais, P. R., Meyer, C., Mandarino, L. J., & Yi, Z. (2009) · Journal of Proteome Research · doi:10.1021/pr9007267 · Cited by 85

Lifelong exercise and mild (8%) caloric restriction attenuate age-induced alterations in plantaris muscle morphology, oxidative stress and IGF-1 in the Fischer-344 rat

Kim, J.-H., Kwak, H., Leeuwenburgh, C., & Lawler, J. M. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2007.12.012 · Cited by 83

1α,25(OH)2D3‐dependent modulation of Akt in proliferating and differentiating C2C12 skeletal muscle cells

Buitrago, C., Arango, N. S., & Boland, R. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23444 · Cited by 79

Role of VDR in 1α,25-dihydroxyvitamin D3-dependent non-genomic activation of MAPKs, Src and Akt in skeletal muscle cells

Buitrago, C., Pardo, V. G., & Boland, R. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.02.013 · Cited by 79

Nutritional strategies to counteract muscle atrophy caused by disuse and to improve recovery

Magne, H., Savary-Auzeloux, I., Rémond, D., & Dardevet, D. (2013) · Nutrition Research Reviews · doi:10.1017/s0954422413000115 · Cited by 78

Inhibition of Myoblast Differentiation by Tumor Necrosis Factor α Is Mediated by c-Jun N-terminal Kinase 1 and Leukemia Inhibitory Factor

Alter, J., Rozentzweig, D., & Bengal, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801379200 · Cited by 77

C2C12 myoblastoma cell differentiation and proliferation is stimulated by androgens and associated with a modulation of myostatin and Pax7 expression

Diel, P. R., Baadners, D., Schlüpmann, K., Velders, M., & Schwarz, J. P. (2008) · Journal of Molecular Endocrinology · doi:10.1677/jme-07-0175 · Cited by 77

Diversity of human skeletal muscle in health and disease: Contribution of proteomics

Gelfi, C., Vasso, M., & Cerretelli, P. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.02.028 · Cited by 79

Associations of functional candidate genes derived from gene‐expression profiles of prenatal porcine muscle tissue with meat quality and muscle deposition

Wimmers, K., Muráni, E., PAS, M. F. W. T., Chang, K., Davoli, R., Merks, J. W. M., Henne, H., Murániová, M., da Costa, N., Harlizius, B., et al. (2007) · Animal Genetics · doi:10.1111/j.1365-2052.2007.01639.x · Cited by 72

Molecular effects of exercise in patients with inflammatory rheumatic disease

Lundberg, I. E., & Nader, G. A. (2008) · Nature Clinical Practice Rheumatology · doi:10.1038/ncprheum0929 · Cited by 72

Effects of IL-10 and age on IL-6, IL-1β, and TNF-α responses in mouse skeletal and cardiac muscle to an acute inflammatory insult

Meador, B. M., Krzyszton, C. P., Johnson, R. W., & Huey, K. A. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01079.2007 · Cited by 72

The role of sex steroid hormones in the pathophysiology and treatment of sarcopenia

Kim, Y. J., Tamadon, A., Park, H. T., Kim, H., & Ku, S. (2016) · Osteoporosis and Sarcopenia · doi:10.1016/j.afos.2016.06.002 · Cited by 76

RAGE Expression in Rhabdomyosarcoma Cells Results in Myogenic Differentiation and Reduced Proliferation, Migration, Invasiveness, and Tumor Growth

Riuzzi, F., Sorci, G., & Donato, R. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070049 · Cited by 64

Insulin-Like Growth Factor I: The Yin and Yang of Muscle Atrophy

Heszele, M. F. C., & Price, S. R. (2004) · Endocrinology · doi:10.1210/en.2004-1037 · Cited by 64

Cyclic Compressive Loading Facilitates Recovery after Eccentric Exercise

Butterfield, T. A., Zhao, Y., Agarwal, S., Haq, F. U., & Best, T. M. (2008) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31816c4e12 · Cited by 63

Biomechanical signals upregulate myogenic gene induction in the presence or absence of inflammation

Chandran, R., Knobloch, T. J., Anghelina, M. I., & Agarwal, S. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00594.2006 · Cited by 62

Ultrasound Modulates the Inflammatory Response and Promotes Muscle Regeneration in Injured Muscles

Nagata, K., Nakamura, T., Fujihara, S., & Tanaka, E. (2013) · Annals of Biomedical Engineering · doi:10.1007/s10439-013-0757-y · Cited by 56

Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation

Yun, B.-G., & Matts, R. L. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.03.003 · Cited by 56

NDRG2, a novel regulator of myoblast proliferation, is regulated by anabolic and catabolic factors

Foletta, V. C., Prior, M. J., Stupka, N., Carey, K. A., Segal, D., Jones, S., Swinton, C., Martin, S. D., Cameron‐Smith, D., & Walder, K. R. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.167882 · Cited by 55

The possible role of myostatin in skeletal muscle atrophy and cachexia

Jespersen, J., Kjær, M., & Schjerling, P. (2005) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2005.00498.x · Cited by 55

Estrogen-related receptor α regulates skeletal myocyte differentiation via modulation of the ERK MAP kinase pathway

Murray, J., & Huss, J. M. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00033.2011 · Cited by 55

Sarcopenia and diabetes: pathogenesis and consequences

Khamseh, M. E., Malek, M., Aghili, R., & Emami, Z. (2011) · The British Journal of Diabetes · doi:10.1177/1474651411413644 · Cited by 51

Hsp90 functions to balance the phosphorylation state of Akt during C2C12 myoblast differentiation

Yun, B.-G., & Matts, R. L. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.006 · Cited by 52

Microarray analysis of the temporal response of skeletal muscle to methylprednisolone: comparative analysis of two dosing regimens

Almon, R. R., DuBois, D. C., Yao, Z., Hoffman, E. P., Ghimbovschi, S. D., & Jusko, W. J. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00242.2006 · Cited by 52

Recovery of skeletal muscle mass after extensive injury: positive effects of increased contractile activity

Richard‐Bulteau, H., Serrurier, B., Crassous, B., Banzet, S., Peinnequin, A., Bigard, X. A., & Koulmann, N. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00355.2007 · Cited by 49

Increased energy expenditure and leptin sensitivity account for low fat mass in myostatin-deficient mice

Choi, S. J., Yablonka‐Reuveni, Z., Kaiyala, K. J., Ogimoto, K., Schwartz, M. W., & Wisse, B. E. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00656.2010 · Cited by 51

Impaired expression of insulin‐like growth factor‐1 system in skeletal muscle of amyotrophic lateral sclerosis patients

Lunetta, C., Serafini, M., Prelle, A. C., Magni, P., Dozio, E., Ruscica, M., Sassone, J., Colciago, C., Moggio, M. G., Corbo, M., et al. (2011) · Muscle & Nerve · doi:10.1002/mus.22288 · Cited by 48

Isolation, characterization, and molecular regulation of muscle stem cells

Fukada, S., Ma, Y., Ohtani, T., Watanabe, Y., Murakami, S., & Yamaguchi, M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00317 · Cited by 48

Folic acid promotes the myogenic differentiation of C2C12 murine myoblasts through the Akt signaling pathway

Hwang, S. Y., Kang, Y. J., Sung, B., Kim, M., Kim, D. H., Lee, Y., Yoo, M., Kim, C. M., Chung, H. Y., & Kim, N. D. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2311 · Cited by 46

The TWEAK-Fn14 System: Breaking the Silence of Cytokine-Induced Skeletal Muscle Wasting

Bhatnagar, S., & Kumar, A. (2011) · Current Molecular Medicine · doi:10.2174/156652412798376107 · Cited by 43

Insight into muscle stem cell regeneration and mechanobiology

Pang, K. T., Loo, L. S. W., Chia, S., Ong, F. Y. T., Yu, H., & Walsh, I. (2023) · Stem Cell Research & Therapy · doi:10.1186/s13287-023-03363-y · Cited by 46

Glutamine prevents myostatin hyperexpression and protein hypercatabolism induced in C2C12 myotubes by tumor necrosis factor-α

Bonetto, A., Penna, F., Minero, V. G., Reffo, P., Costamagna, D., Bonelli, G., Baccino, F. M., & Costelli, P. (2010) · Amino Acids · doi:10.1007/s00726-010-0683-3 · Cited by 45

The influence of platelet-rich plasma on myogenic differentiation

McClure, M. J., Garg, K., Simpson, D. G., Ryan, J. J., Sell, S. A., Bowlin, G. L., & Ericksen, J. J. (2013) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.1755 · Cited by 43

Emerging drugs for sarcopenia: age-related muscle wasting

Lynch, G. S. (2004) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.9.2.345 · Cited by 45

Regulation of REDD1 by insulin‐like growth factor‐I in skeletal muscle and myotubes

Frost, R. A., Huber, D. S., Pruznak, A. M., & Lang, C. H. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22349 · Cited by 42

Systemic delivery of NEMO binding domain/IKKγ inhibitory peptide to young mdx mice improves dystrophic skeletal muscle histopathology

Reay, D. P., Yang, M. L., Watchko, J. F., Daood, M., O’Day, T. L., Rehman, K. K., D, D. C. G., Robbins, P. D., & Clemens, P. R. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.05.008 · Cited by 41

The Effects of Creatine Monohydrate Supplementation With and Without D-Pinitol on Resistance Training Adaptations

Kerksick, C. M., Wilborn, C. D., Campbell, W. I., Harvey, T. M., Marcello, B. M., Roberts, M. D., Parker, A. G., Byars, A. G., Greenwood, L. D., Almada, A. L., et al. (2009) · Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e3181b3e0de · Cited by 39

Dose-dependent modulation of myogenesis by HGF: implications for c-Met expression and downstream signalling pathways

Walker, N. L., Kahamba, T., Woudberg, N. J., Goetsch, K. P., & Niesler, C. U. (2015) · Growth Factors · doi:10.3109/08977194.2015.1058260 · Cited by 39

Paracrine Release of Insulin-Like Growth Factor 1 from a Bioengineered Tissue Stimulates Skeletal Muscle Growth in Vitro

Shansky, J., Creswick, B., Lee, P. H. U., Wang, X. Q., & Vandenburgh, H. H. (2006) · Tissue Engineering · doi:10.1089/ten.2006.12.1833 · Cited by 37

Cancer Cachexia Pathophysiology and Translational Aspect of Herbal Medicine

Suzuki, H., Asakawa, A., Amitani, H., Fujitsuka, N., Nakamura, N., & Inui, A. (2013) · Japanese Journal of Clinical Oncology · doi:10.1093/jjco/hyt075 · Cited by 36

Challenges in drug development for muscle disease: A stakeholders' meeting

Mendell, J. R., Csimma, C., McDonald, C. M., Escolar, D. M., Janis, S., Porter, J. D., Hesterlee, S. E., & Howell, R. R. (2006) · Muscle & Nerve · doi:10.1002/mus.20686 · Cited by 35

GIT2—A keystone in ageing and age-related disease

van Gastel, J., Boddaert, J., Jushaj, A., Premont, R. T., Luttrell, L. M., Janssens, J., Martin, B., & Maudsley, S. R. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.02.002 · Cited by 32

Regulation of MMP and TIMP expression in synovial fibroblasts from knee osteoarthritis with flexion contracture using adenovirus-mediated relaxin gene therapy

Ko, J. H., Kang, Y. M., Yang, J., Kim, J. S., Lee, W. J., Kim, S. H., Yang, I. H., & Moon, S. H. (2019) · The Knee · doi:10.1016/j.knee.2019.01.010 · Cited by 31

MEAT SCIENCE AND MUSCLE BIOLOGY SYMPOSIUM—Mechanism of growth hormone stimulation of skeletal muscle growth in cattle1

Jiang, H., & Ge, X. (2013) · Journal of Animal Science · doi:10.2527/jas.2013-7095 · Cited by 36

MyoD- and nerve-dependent maintenance of MyoDexpression in mature muscle fibres acts through the DRR/PRR element

CHARGÉ, S. B. P., Brack, A. S., Bayol, S. A., & Hughes, S. M. (2008) · BMC Developmental Biology · doi:10.1186/1471-213x-8-5 · Cited by 28

Disuse Atrophy of Human Skeletal Muscle

Urso, M. L. (2009) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181a6458a · Cited by 29

PKR is a novel functional direct player that coordinates skeletal muscle differentiation via p38MAPK/AKT pathways

Alisi, A., Spaziani, A., Anticoli, S., Ghidinelli, M., & Balsano, C. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.11.006 · Cited by 28

Long‐term exercise training prevents mammary tumorigenesis‐induced muscle wasting in rats through the regulation of TWEAK signalling

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Comprehensive Medical Science,

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