Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1

Identification of ubiquitin ligases required for skeletal muscle atrophy.

Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148

Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression

Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539

IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice

Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367

The SCF ubiquitin ligase: insights into a molecular machine

Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114

The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle

Clarke, B. A., Drujan, D., Willis, M. S., Murphy, L. O., Corpina, R. A., Burova, E., Rakhilin, S. V., Stitt, T. N., Patterson, C., Latres, E., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.009 · Cited by 683

Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases

Sacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585

Patterns of gene expression in atrophying skeletal muscles: response to food deprivation

Jagoe, R. T., Lecker, S. H., Gomes, M., & Goldberg, A. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0312com · Cited by 344

Role of Inactivity in Chronic Diseases: Evolutionary Insight and Pathophysiological Mechanisms

Booth, F. W., Roberts, C. K., Thyfault, J. P., Ruegsegger, G. N., & Toedebusch, R. G. (2017) · Physiological Reviews · doi:10.1152/physrev.00019.2016 · Cited by 696

The Role of Inflammation in Age-Related Sarcopenia

Dalle, S., Rossmeislova, L., & Koppo, K. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01045 · Cited by 668

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

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

Lipid modulation of skeletal muscle mass and function

Lipina, C., & Hundal, H. S. (2017) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12144 · Cited by 247

Age-related differences in lean mass, protein synthesis and skeletal muscle markers of proteolysis after bed rest and exercise rehabilitation

Tanner, R. E., Brunker, L. B., Agergaard, J., Barrows, K. M., Briggs, R. A., Kwon, O. S., Young, L. M., Hopkins, P. N., Volpi, E., Marcus, R. L., et al. (2015) · The Journal of Physiology · doi:10.1113/jp270699 · Cited by 223

OPA1 deficiency promotes secretion of FGF21 from muscle that prevents obesity and insulin resistance

Pereira, R. O., Tadinada, S. M., Zasadny, F. M., Oliveira, K. J., Pires, K. M. P., Olvera, A., Jeffers, J., Souvenir, R., Mcglauflin, R., Seei, A., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696179 · Cited by 211

Indoxyl sulfate potentiates skeletal muscle atrophy by inducing the oxidative stress-mediated expression of myostatin and atrogin-1

Enoki, Y., Watanabe, H., Arake, R., Sugimoto, R., Imafuku, T., Tominaga, Y., Ishima, Y., Kotani, S., Nakajima, M., Tanaka, M., et al. (2016) · Scientific Reports · doi:10.1038/srep32084 · Cited by 188

FoxO Transcription Factors Are Critical Regulators of Diabetes-Related Muscle Atrophy

O’Neill, B. T., Bhardwaj, G., Penniman, C. M., Krumpoch, M. T., Suarez Beltran, P. A., Klaus, K., Poro, K., Li, M., Pan, H., Dreyfuss, J. M., et al. (2019) · Diabetes · doi:10.2337/db18-0416 · Cited by 167

Integrin signaling: linking mechanical stimulation to skeletal muscle hypertrophy

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

Partial Inhibition of mTORC1 in Aged Rats Counteracts the Decline in Muscle Mass and Reverses Molecular Signaling Associated with Sarcopenia

Joseph, G. A., Wang, S. X., Jacobs, C. E., Zhou, W., Kimble, G. C., Tse, H. W., Eash, J. K., Shavlakadze, T., & Glass, D. J. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00141-19 · Cited by 158

Lipid metabolism in sarcopenia

Al Saedi, A., Debruin, D. A., Hayes, A., & Hamrick, M. (2022) · Bone · doi:10.1016/j.bone.2022.116539 · Cited by 140

Regulation of mTORC1 by growth factors, energy status, amino acids and mechanical stimuli at a glance

Bond, P. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0118-y · Cited by 121

Yes‐Associated Protein is up‐regulated by mechanical overload and is sufficient to induce skeletal muscle hypertrophy

Goodman, C. A., Dietz, J. M., Jacobs, B. L., McNally, R. M., You, J.-S., & Hornberger, T. A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.04.047 · Cited by 121

Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation

Haberecht-Müller, S., Krüger, E., & Fielitz, J. (2021) · Biomolecules · doi:10.3390/biom11091327 · Cited by 108

Amino acid sensing in skeletal muscle

Moro, T., Ebert, S. M., Adams, C. M., & Rasmussen, B. B. (2016) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2016.06.010 · Cited by 104

A Key Role for the Ubiquitin Ligase UBR4 in Myofiber Hypertrophy in Drosophila and Mice

Hunt, L. C., Stover, J., Haugen, B., Shaw, T. I., Li, Y., Pagala, V. R., Finkelstein, D., Barton, E. R., Fan, Y., Labelle, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.094 · Cited by 90

FoxO‐dependent atrogenes vary among catabolic conditions and play a key role in muscle atrophy induced by hindlimb suspension

Brocca, L., Toniolo, L., Reggiani, C., Bottinelli, R., Sandri, M., & Pellegrino, M. A. (2017) · The Journal of Physiology · doi:10.1113/jp273097 · Cited by 93

Long acting GLP-1 analog liraglutide ameliorates skeletal muscle atrophy in rodents

Gurjar, A. A., Kushwaha, S., Chattopadhyay, S., Das, N., Pal, S., China, S. P., Kumar, H., Trivedi, A. K., Guha, R., Chattopadhyay, N., et al. (2020) · Metabolism · doi:10.1016/j.metabol.2019.154044 · Cited by 79

Endurance Exercise Enhances the Effect of Strength Training on Muscle Fiber Size and Protein Expression of Akt and mTOR

Kazior, Z., Willis, S. J., Moberg, M., Apró, W., Calbet, J. A. L., Holmberg, H.-C., & Blomstrand, E. (2016) · PLOS ONE · doi:10.1371/journal.pone.0149082 · Cited by 82

Polyphenols and Their Potential Role in Preventing Skeletal Muscle Atrophy

Salucci, S., & Falcieri, E. (2020) · Nutrition Research · doi:10.1016/j.nutres.2019.11.004 · Cited by 83

Skeletal Muscle Atrophy: Discovery of Mechanisms and Potential Therapies

Ebert, S. M., Al-Zougbi, A., Bodine, S. C., & Adams, C. M. (2019) · Physiology · doi:10.1152/physiol.00003.2019 · Cited by 80

Dkk3 dependent transcriptional regulation controls age related skeletal muscle atrophy

Yin, J., Yang, L., Xie, Y., Liu, Y., Li, S., Yang, W., Xu, B., Ji, H., Ding, L., Wang, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04038-6 · Cited by 72

Exercise and the regulation of skeletal muscle hypertrophy

McGlory, C., & Phillips, S. M. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.06.018 · Cited by 69

Dihydromyricetin Attenuates Dexamethasone-Induced Muscle Atrophy by Improving Mitochondrial Function Via the PGC-1α Pathway

Huang, Y., Chen, K., Ren, Q., Yi, L., Zhu, J., Zhang, Q., & Mi, M. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000493040 · Cited by 64

How the love of muscle can break a heart: Impact of anabolic androgenic steroids on skeletal muscle hypertrophy, metabolic and cardiovascular health

McCullough, D., Webb, R., Enright, K. J., Lane, K. E., McVeigh, J., Stewart, C. E., & Davies, I. G. (2021) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-020-09616-y · Cited by 62

Effects of skeletal muscle energy availability on protein turnover responses to exercise

Smiles, W. J., Hawley, J. A., & Camera, D. M. (2016) · Journal of Experimental Biology · doi:10.1242/jeb.125104 · Cited by 48

“Get the Balance Right”: Pathological Significance of Autophagy Perturbation in Neuromuscular Disorders

Castets, P., Frank, S., Sinnreich, M., & Rüegg, M. A. (2016) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-160153 · Cited by 49

Inhibition of myostatin prevents microgravity-induced loss of skeletal muscle mass and strength

Smith, R. C., Cramer, M. S., Mitchell, P. J., Lucchesi, J., Ortega, A. M., Livingston, E. W., Ballard, D., Zhang, L., Hanson, J., Barton, K., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0230818 · Cited by 48

Myostatin/Activin Receptor Ligands in Muscle and the Development Status of Attenuating Drugs

Rodgers, B. D., & Ward, C. W. (2022) · Endocrine Reviews · doi:10.1210/endrev/bnab030 · Cited by 111

Effects of different modes of exercise on skeletal muscle mass and function and IGF-1 signaling during early aging in mice

Li, B., Feng, L., Wu, X., Cai, M., Yu, J. J., & Tian, Z. (2022) · Journal of Experimental Biology · doi:10.1242/jeb.244650 · Cited by 45

HDAC7-mediated control of tumour microenvironment maintains proliferative and stemness competence of human mammary epithelial cells

Cutano, V., Di Giorgio, E., Minisini, M., Picco, R., Dalla, E., & Brancolini, C. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12503 · Cited by 44

Inflammation and metabolism: the role of adiposity in sarcopenic obesity

Lynch, G. M., Murphy, C. H., Castro, E. D. M., & Roche, H. M. (2020) · Proceedings of the Nutrition Society · doi:10.1017/s0029665120007119 · Cited by 41

Camphene Attenuates Skeletal Muscle Atrophy by Regulating Oxidative Stress and Lipid Metabolism in Rats

Baek, S., Kim, J., Moon, B. S., Park, S. M., Jung, D. E., Kang, S. Y., Lee, S. J., Oh, S. J., Kwon, S. H., Nam, M. H., et al. (2020) · Nutrients · doi:10.3390/nu12123731 · Cited by 39

Epigenetics of Muscle- and Brain-Specific Expression of KLHL Family Genes

Ehrlich, K. C., Baribault, C., & Ehrlich, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218394 · Cited by 35

Resveratrol Attenuates Denervation-Induced Muscle Atrophy Due to the Blockade of Atrogin-1 and p62 Accumulation

Asami, Y., Aizawa, M., Kinoshita, M., Ishikawa, J., & Sakuma, K. (2018) · International Journal of Medical Sciences · doi:10.7150/ijms.22723 · Cited by 33

Master Regulators of Muscle Atrophy: Role of Costamere Components

Gorza, L., Sorge, M., Seclì, L., & Brancaccio, M. (2021) · Cells · doi:10.3390/cells10010061 · Cited by 31

D-Methionine Ameliorates Cisplatin-Induced Muscle Atrophy via Inhibition of Muscle Degradation Pathway

Wu, C.-T., Liao, J.-M., Ko, J.-L., Lee, Y.-L., Chang, H.-Y., Wu, C.-H., & Ou, C.-C. (2019) · Integrative Cancer Therapies · doi:10.1177/1534735419828832 · Cited by 32

Muscle‐specific Perilipin2 down‐regulation affects lipid metabolism and induces myofiber hypertrophy

Conte, M., Armani, A., Conte, G., Serra, A., Franceschi, C., Mele, M., Sandri, M., & Salvioli, S. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12355 · Cited by 30

Mountain Ginseng Inhibits Skeletal Muscle Atrophy by Decreasing Muscle Ring finger Protein-1 and Atrogin1 through Forkhead Box O3 in L6 Myotubes

Seok, Y. M., Yoo, J.-M., Nam, Y., Kim, J., Kim, J. S., Son, J.-H., & Kim, H. J. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113557 · Cited by 27

E3 ubiquitin ligases and their therapeutic potential in disease Management

Madhukar, G., Haque, M. A., Khan, S., Kim, J.-J., & Danishuddin (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116875 · Cited by 26

The Extract of Arctium lappa L. Fruit (Arctii Fructus) Improves Cancer-Induced Cachexia by Inhibiting Weight Loss of Skeletal Muscle and Adipose Tissue

Han, Y.-H., Mun, J.-G., Jeon, H. D., Yoon, D. H., Choi, B.-M., Kee, J.-Y., & Hong, S.-H. (2020) · Nutrients · doi:10.3390/nu12103195 · Cited by 24

Ubiquitin E3 ligase Atrogin-1 protein is regulated via the rapamycin-sensitive mTOR-S6K1 signaling pathway in C2C12 muscle cells

Nishimura, Y., Chunthorng-Orn, J., Lord, S., Musa, I., Dawson, P., Holm, L., & Lai, Y.-C. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00384.2021 · Cited by 23

Neuromuscular electrical stimulation prior to presleep protein feeding stimulates the use of protein-derived amino acids for overnight muscle protein synthesis

Dirks, M. L., Groen, B. B. L., Franssen, R., van Kranenburg, J., & van Loon, L. J. C. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00331.2016 · Cited by 22

Short-Term Creatine Supplementation Changes Protein Metabolism Signaling in Hindlimb Suspension

Marzuca-Nassr, G. N., Fortes, M. A. S., Guimarães-Ferreira, L., Murata, G. M., Vitzel, K. F., Vasconcelos, D. A. A., Bassit, R. A., & Curi, R. (2019) · Brazilian Journal of Medical and Biological Research · doi:10.1590/1414-431x20198391 · Cited by 19

Muscle Proteolytic System Modulation through the Effect of Taurine on Mice Bearing Muscular Atrophy

Khalil, R. M., Abdo, W. S., Saad, A., & Khedr, E. G. (2018) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3240-5 · Cited by 19

The Signature of MicroRNA Dysregulation in Muscle Paralyzed by Spinal Cord Injury Includes Downregulation of MicroRNAs that Target Myostatin Signaling

De Gasperi, R., Graham, Z. A., Harlow, L. M., Bauman, W. A., Qin, W., & Cardozo, C. P. (2016) · PLOS ONE · doi:10.1371/journal.pone.0166189 · Cited by 19

Regulation of the early expression of MAFbx/atrogin-1 and MuRF1 through membrane-initiated cortisol action in the skeletal muscle of rainbow trout

Aravena-Canales, D., Aedo, J. E., Molina, A., & Valdés, J. A. (2021) · Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2021.110565 · Cited by 15

Dioscorea Nipponica Extracts Enhance Recovery from Skeletal Muscle Atrophy by Suppressing NF-κB Expression

Park, K.-S., Kim, H. J., Hwang, J. T., & Ko, B. S. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.104109 · Cited by 8

Protein Supplementation Enhances the Effects of Intermittent Loading on Skeletal Muscles by Activating the mTORC1 Signaling Pathway in a Rat Model of Disuse Atrophy

Miyatake, S., Hino, K., Natsui, Y., Ebisu, G., & Fujita, S. (2020) · Nutrients · doi:10.3390/nu12092729 · Cited by 7