The ubiquitin–proteasome system in regulation of the skeletal muscle homeostasis and atrophy: from basic science to disorders

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351

Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury

Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,304

Autophagy regulates lipid metabolism

Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975

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

The role of autophagy during the early neonatal starvation period

Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865

Integration of proteomic and genetic approaches to assess developmental muscle atrophy

Brooks, D. S., Vishal, K., Bawa, S., Alder, A., & Geisbrecht, E. R. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.242698 · Cited by 4

Disruption of male fertility-critical Dcaf17 dysregulates mouse testis transcriptome

Abu‐Dawud, R., Mistry, B. V., Rajab, M., Alanazi, M., Al‐Yacoub, N., Kashir, J., Almohanna, F., Çolak, D., & Assiri, A. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-25826-7 · Cited by 3

Skeletal muscle atrophy in pulmonary arterial hypertension: potential mechanisms and effects of physical exercise

Costa, S. F. F., Soares, L. L., Leite, L. B., Portes, A. M. O., & Natali, A. J. (2025) · Heart Failure Reviews · doi:10.1007/s10741-025-10539-6 · Cited by 3

Linking Biomarkers with Causes, Lifestyle Factors, and Management of Sarcopenia

Papadopoulou, S. Κ., Voulgaridou, G., Papadimitriou, K., & Koidou, E. (2022) · Biomarkers in disease · doi:10.1007/978-3-030-81304-8_64-1 · Cited by 3

Arachidonic Acid Protects Skeletal Muscle Against Hyperglycaemia‐Induced Muscle Atrophy by Modulating Myogenesis and Regulating KLF15 Expression in C57Bl /6 Mice

Mitra, A., Chaudhury, D., Rai, A. B., Das, U. N., Prasad, T. S. K., Bose, B., & Sudheer Shenoy, P. (2025) · The FASEB Journal · doi:10.1096/fj.202502321rr · Cited by 2

Multi-tissue spatial transcriptomics identified simultaneous responses to oxidative stress and apoptosis in parallel with tissue-specific reprogramming in modeled chronic kidney disease-mineral and bone disorder

Hibbard, L. M., Liu, S., Marambio, Y. G., Jennings, K. N., Welc, S. S., Wan, J., & White, K. E. (2025) · JBMR Plus · doi:10.1093/jbmrpl/ziaf161 · Cited by 2

Metabolic Reprogramming in Cancer Cachexia

Ibrahim, M., Gomez-Jenkins, M., & White, E. (2025) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-070924-011243 · Cited by 3

Cancer targeting carfilzomib nanomedicine: a comprehensive review of delivery vehicles and efficacy

Molinaro, M., & Pan, D. (2025) · Nanomedicine · doi:10.1080/17435889.2025.2579621 · Cited by 2

HSALR Mice Exhibit Co-Expression of Proteostasis Genes Prior to Development of Muscle Weakness

Lazic, D. M., Jovanovic, V. M., Karanović, J., Pavicevic, D. S., & Jovanovic, B. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110793 · Cited by 2

DR8 (DHNNPQIR), a rapeseed-derived peptide, mitigates fibrosis and muscle atrophy in chronic kidney disease by targeting CNR1–ERK/ELK-1 signaling

Zhang, W., Zuo, Y., Xu, D., Lin, Y., Zang, Y., Chen, R., Chen, M., & Su, Z. (2025) · Peptides · doi:10.1016/j.peptides.2025.171456 · Cited by 2

Molecular Bases of Myopathies and Their Impact on Clinical Practice: Advances and Future Perspectives

Campuzano-Donoso, M., Reytor-González, C., Toral-Noristz, M., González, Y., & Simancas‐Racines, D. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27031392 · Cited by 2

Neuromuscular Mechanisms and Oxidative Stress in Skeletal Muscle Atrophy: Emerging Stem Cell and Gene-Based Therapeutic Strategies

Gunasekaran, S. K., Khan, M. A., Mirza, M. A., Bhupathi, S. S., & Azeeze, M. S. T. A. (2026) · Muscles · doi:10.3390/muscles5010013 · Cited by 2

Formoterol reduces muscle wasting in mice undergoing doxorubicin chemotherapy

de Lima, E. A., Teixeira, A. A. D. S., Silveira, L. S., Jové, Q., Ladrón, N. Á., Pereira, M. G., López-Soriano, F. J., Argilés, J. M. A., Brum, P. C., Busquets, S., et al. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2023.1237709 · Cited by 2

Krill oil attenuates obesity-induced skeletal muscle atrophy in mice

Zhou, M., Yang, Y., Zheng, Y., Wu, Z., Chen, C., Liang, Q., Yang, Y., Wu, H., Guo, X., & Du, L. (2024) · Food Science and Human Wellness · doi:10.26599/fshw.2024.9250018 · Cited by 2

JAG1 overexpression partially rescues muscle function in a zebrafish model of duchenne muscular dystrophy

Nesari, V., Balakrishnan, S., & Nongthomba, U. (2024) · Journal of Genetics · doi:10.1007/s12041-024-01489-3 · Cited by 2

Identification of chemical scaffolds for targeting ubiquitin-specific protease 11 (USP11) through high-throughput virtual screening

Lee, H., Hurh, S., Kang, S., Yoon, J., Hwang, J., Logan, D. T., & Kim, H. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2518191 · Cited by 2

Reduced muscle expression heterogeneity by categorising diabetic subjects resulted in improved statistical significance for trascriptome comparison

Kumar, R., Niharika, M. V. S., Kushwaha, P., Ojha, K. K., Yadav, H. N., Sharma, N., & Singh, V. K. (2024) · Human Gene · doi:10.1016/j.humgen.2024.201283 · Cited by 1

Transcriptomic Insights into Post-Spawning Death and Muscle Atrophy in Ayu (Plecoglossus altivelis)

Liang, J., Fujisawa, M., Toma, S., Asakawa, S., Yoshitake, K., Igarashi, Y., Saito, S., Akutsu, T., Suzuki, K., & Kinoshita, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020434 · Cited by 1

Role of molecular chaperones and co-chaperones in maintaining proteostasis

Naik, R. A., Rajpoot, R., Gupta, N., Dash, D., Dubey, V., Koiri, R. K., & Singh, S. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-18716-2.00006-5 · Cited by 1

Gardenia Fruit and Its Active Compound Crocin Protect Against Dexamethasone‐Induced Muscle Atrophy via Nrf2 Activation

Kim, J.-I., Jeong, H. Y., Kim, Y. I., Yoo, A., Lee, H., Jung, C. H., & Ahn, J. (2025) · Journal of Food Biochemistry · doi:10.1155/jfbc/2952670 · Cited by 1

Coupled Bone–Muscle Degeneration in Chronic Pancreatitis: A Juvenile Porcine Model of Secondary Osteosarcopenia

Muszyński, S., Świetlicki, M., Wojtysiak, D., Grzegorzewska, A. K., Dobrowolski, P., Świątkiewicz, M., Arciszewski, M. B., Puzio, I., Bonior, J., Tomczyk‐Warunek, A., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167690 · Cited by 1

Effects of Dietary Black Soldier Fly (Hermetia illucens) Oil Supplementation on Flesh Quality of Largemouth Bass (Micropterus salmoides)

Wang, Z.-C., Cao, Y., Yang, W., Wang, Z.-T., Kuang, Y., Wu, P., Cai, C.-F., & Ye, Y.-T. (2025) · Fishes · doi:10.3390/fishes10110548 · Cited by 1

Resistance exercise training attenuates skeletal muscle atrophy in experimental pulmonary arterial hypertension

Costa, S. F. F., Leite, L. B., Soares, L. L., Generoso, S. C. D. L., Xavier, M. A. M., Faria, M. S., Quintão, A. E. D. C., Guimarães‐Ervilha, L. O., Lima, T. I., Pelozin, B. R. D. A., et al. (2025) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-025-03142-z · Cited by 1

Cachexia, sarcopenia, malnutrition and their impact on survival, treatment toxicities, and quality of life in locally advanced cervical cancer patients undergoing concomitant chemoradiotherapy: A scoping review

Martinelli, C. V., Ercoli, A., Alfano, L., Pentimalli, F., Mazzarotti, G., Ferrantelli, G., LORENZO, A. D., Esposito, T., Giordano, A., & Cortellino, S. (2025) · Clinical Nutrition Open Science · doi:10.1016/j.nutos.2025.100620 · Cited by 1

Targeting muscle wasting: Bioinformatics-derived ubiquitination genes as potential therapeutic targets for sarcopenia

Liu, X., Li, R., & Kuang, Y. (2026) · Medicine · doi:10.1097/md.0000000000047161 · Cited by 2

CHK2-USP37 axis stabilizes FOXO4 to sustain senescence and evade apoptosis

Sun, J., Geng, A., Song, Z., Chen, L., Zhang, Z.-N., Jiang, Y., & Mao, Z. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2526252123 · Cited by 1

Mechanistic actions of eldecalcitol and alfacalcidol across the muscle-metabolic axis: A selectivity perspective in sarcopenia and type 2 diabetes

Cambria, M. T., Campanella, M., Russo, C., Agafonova, A., Surdo, S., Valle, M. S., & Malaguarnera, L. (2026) · iScience · doi:10.1016/j.isci.2026.115945 · Cited by 1

Sustaining Muscle, Cardiovascular Health, and the Environment: Is Plant-Based Protein the Key?

Cannito, T., Ivetac, A., Fiotti, N., Mearelli, F., Bella, S. D., Girolamo, F. G. D., & Biolo, G. (2026) · Nutrients · doi:10.3390/nu18091446 · Cited by 1

Dysregulation of the ubiquitin–proteasome system in aging skeletal muscle

Song, G., Lee, B.-Y., & Baek, K. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119504 · Cited by 2

Shikimic acid ameliorates immobilization-induced muscle atrophy through regulation of inflammation and muscle protein homeostasis

Kim, M., Yoo, J., Moon, C. Y., Hwang, J.-K., & Kang, H. (2026) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2026.110434 · Cited by 1

The cGAS–STING pathway contributes to cisplatin-induced skeletal muscle atrophy through altered proteostasis and myogenic signaling

Liu, X., Xu, M., Wang, H., Wang, H., Wang, H., Fang, W., Li, M., Huang, J., Chen, F. C., Wang, H., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02989-8 · Cited by 1

Ubiquitin Ligases in pro-atrophic and antiatrophic signaling cascades in muscles

Singh, A. K., & Rathee, V. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12239-2 · Cited by 1

Proteomic Analysis of Glucose-Induced Cardiac Myoblasts and the Potential Role of mir-92b-5p in Regulating Sarcomere Proteins Under a Hyperglycemic Environment

Mathur, P., & Rani, V. (2022) · Protein and Peptide Letters · doi:10.2174/0929866529666220819121325 · Cited by 1

Resistance exercise exacerbates muscle atrophy of skeletal muscle-specific Beclin1 conditioned knockout (cKO) mice

Zeng, Z., Zhang, H., Liang, J., Lv, J., Wu, L., & Chen, N. (2024) · Advanced Exercise and Health Science · doi:10.1016/j.aehs.2024.03.001 · Cited by 2

The Influence of Stress and Binge-Patterned Alcohol Drinking on Mouse Skeletal Muscle Protein Synthesis and Degradation Pathways

Reed, C. H., Tystahl, A. C., Eo, H., Buhr, T. J., Bauer, E. E., Lee, J. H., Clark, P., & Valentine, R. J. (2024) · Biomolecules · doi:10.3390/biom14050527 · Cited by 2

Exercise training for patients with heart failure and preserved ejection fraction. A narrative review

Caminiti, G., Volterrani, M., Iellamo, F., Marazzi, G., Silvestrini, M., Giamundo, D. M., Morsella, V., Biasio, D. D., Franchini, A., & Perrone, M. A. (2024) · Monaldi Archives for Chest Disease · doi:10.4081/monaldi.2024.3030 · Cited by 1

Alterations in FoxO3a, NF-κB, and MuRF1 Expression in the Soleus Muscle of Male Rats Following High-Intensity Interval Training and Detraining

Sheibani, S., Daryanoosh, F., & Zarifkar, A. H. (2024) · Doklady Biochemistry and Biophysics · doi:10.1134/s1607672924600817 · Cited by 1

Linking Biomarkers with Causes, Lifestyle Factors, and Management of Sarcopenia

Papadopoulou, S. Κ., Voulgaridou, G., Papadimitriou, K., & Koidou, E. (2022) · Biomarkers in disease · doi:10.1007/978-3-031-07389-2_64 · Cited by 1

Metabolic and proteomic pathways in muscle involved in beef tenderness development

Schulte, M. D. (2022) · doi:10.31274/td-20240329-502 · Cited by 1

Brains and brawn: Stress-induced myokine abates nervous system aging

Tsui, C. K., Dishart, J. G., & Dillin, A. G. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.05.007

DNA methylation feature differences by gender in sarcopenia using data from the Korean Genome and Epidemiology StudyPreprint

Lee, S.-Y., Gim, J., Kim, S. C., Baek, K., & Yoo, J. (2022) · Research Square · doi:10.21203/rs.3.rs-2103290/v1

The E3 Ubiquitin Ligase Nedd4L Acts as a Checkpoint Against Activation in Quiescent Muscle Stem CellsPreprint

Blackburn, D. M., Sahinyan, K., Hernández-Corchado, A., Lazure, F., Richard, V. R., Raco, L., Perron, G., Zahedi, R. P., Lepper, C., Lepper, C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.10.540205

The effects of exercise on post-burn muscle wasting

Dombrecht, D. (2024) · doi:10.63028/10067/2031330151162165141

The Effect of Combined Exercise on the Expression of FoxO and Atrogin Pathway Genes in the Gastrocnemius and Soleus Muscles of Elderly Rats

Pahlevanzadeh, M., Shabani, R., & Elmieh, A. (2024) · مجله دانشگاه علوم پزشکی جیرفت. · doi:10.61186/jjums.11.1.1512

Transcriptomic Analysis Reveals MSTN Mutations and Mechanisms of Muscle Hypertrophy in a New Guinea Pig BreedPreprint

Carmen-Sifuentes, S., Chauca, L., Yalta, C., Alvarado, E., & Mellisho, E. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.09.627469

Cancer Cachexia: Causes and Therapeutic Strategies

Al-Janabi, I. I. (2025) · Al-Rafidain Journal of Medical Sciences · doi:10.54133/ajms.v8i2.1616

Circadian control of cellular constituent turnover and growth

Kelu, J. J. (2025) · Current Opinion in Physiology · doi:10.1016/j.cophys.2025.100837

Changes in the muscle growth and regulatory factors, TNF-α and Toll-like Receptors 2 and 4 during Exercise, Muscle Atrophy, and Recovery in the Mouse Hind Limb Suspension ModelPreprint

Al‐Zghoul, M. B., Al‐Nassan, S., AL-Abedallat, Q. M., Mayyas, M., Al-Zghoul, A. M., Al-Bdoor, M., & Abu-Salih, A. Q. (2025) · Research Square · doi:10.21203/rs.3.rs-7180388/v1

Muscle-Liver Crosstalk and Sarcopenia

Pérez-Torres, D., & Canas-Pérez, I. (2025) · Springer eBooks · doi:10.1007/978-3-032-01024-7_19

Uncertainty-Aware Gene Rankings Reveal Key Players in Coexpression NetworksPreprint

Mahapatra, S., Subramanian, N. A., & Narayanan, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.13.694156

Trichosanthes kirilowii Maximowicz attenuates dexamethasone induced atrophy in C2C12 myotubes through a Sirtuin 1 associated mechanism

Kim, H., Hong, J. Y., Yeo, C., Jeon, W., Kim, H., Lee, J., Lee, Y. J., & Ha, I. (2025) · Scientific Reports · doi:10.1038/s41598-025-28257-2 · Cited by 1

Pathological Mechanism and Drug Prevention and Treatment of Skeletal Muscle Atrophy

李, 雯. (2025) · Pharmacy Information · doi:10.12677/pi.2026.151004

Comparative proteomic study of muscle tissue of wild boars and domestic pig breeds.

Chernukha, I. M., Ковалев, Л. И., Markov, N. I., Kotenkova, E., Vasilevskaya, E. R., Spirina, M. E., Polishchuk, E. K., & Fedulova, L. (2026) · Theory and practice of meat processing · doi:10.21323/2414-438x-2025-10-4-338-350

Selective activation of the unfolded protein response and proteolytic pathways in sarcopenic limb muscles of bronchiectasis patients

Núñez-Robainas, A., Solano, A., Marsico, S., Alvarado-Miranda, M., Gargallo, C. C., Sáinz, M., Maiques, J. M., & Barreiro, E. (2026) · ERJ Open Research · doi:10.1183/23120541.00746-2025

Focal Estrogen Therapy in Male Rats Promotes Neuronal Survival and Reduces Denervation Atrophy After Spinal Cord Injury via Modulation of β-Catenin and NF-κB

Haque, A., Zaman, V., Drasites, K. P., Sawant, S., Vertegel, A. A., Varma, A. K., Green, C., & Banik, N. L. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04700-2

Identification of new levers to fight muscle atrophy : benefit of the hibernating brown bear model

Cussonneau, L. (2022) · theses.fr (ABES) · doi:10.70675/1a11a81bzf829z4ba2zba9az6f3f4841c773

Déconditionnement du muscle strié squelettique chez la patiente atteinte d’un cancer du sein traité par chimiothérapie : étude de la fonction, des mécanismes cellulaires et d’une contremesure par exercice excentrique

Mallard, J. (2022) · theses.fr (ABES) · doi:10.70675/f8b2c96bzc4cdz4249z8e59z5f87c7ca2462

Gut–muscle axis: A new perspective on microgravity‑induced skeletal muscle atrophy

Hou, W., Wang, L., Hu, S., & Luo, L. (2026) · Life Sciences in Space Research · doi:10.1016/j.lssr.2026.04.006

ER stress: A putative therapeutic target for diabetes mellitus

Anto, E. M., Adheena, M., & Jayamurthy, P. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153773

Coordinated Bone–Muscle Axis Association in South China Carp (Cyprinus carpio rubrofuscus) with Low Bone Mineral Density: An Integrated Analysis of Muscle Texture, Nutrition, Ultrastructure, and Proteomics

Zhao, K., Zhong, Z., Fan, J., Tian, Y., Shi, J., Ma, D., & Zhu, H. (2026) · Foods · doi:10.3390/foods15111860

Aerobic exercise attenuates sarcopenia-related changes via TXNIP-associated modulation of apoptosis, inflammation and autophagy

Zhao, X., Chen, Q., You, J., An, Z., Li, J., Yu, L., & Xu, Z. (2026) · Biochimie · doi:10.1016/j.biochi.2026.05.007

Regulation of Myogenic Cell Apoptosis, UPS, and Autophagy During Mammalian Skeletal Myogenesis

Yue, B., Hu, W., Zhu, S., Chen, D., 关焕玉, Zhao, Z., Wang, H., Wang, J., Zhong, J., & Shi, H. (2026) · Cells · doi:10.3390/cells15121061

Low-dose MyoAAV 2A-mediated delivery of engineered micro-utrophin achieves pan- muscle tissue distribution with elevated muscle function in Duchenne muscular dystrophy

Li, N., Li, Z., Zhang, Z., Xiahou, Z., Xiao, H., Wu, S., Xu, F., Liu, Q., Wu, Y., & Song, Y. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08483-6

Leucine Aminopeptidase 3 Regulates Skeletal Muscle Mitochondrial Homeostasis with Sex-Dependent Metabolic ConsequencesPreprint

Osana, S., Murakami, R., Natsuyama, R., Tabuchi, A., Kano, R., Baba, K., Wang, H., Takada, H., Suzuki, N., Murayama, K., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.20.733486

“Should I stay or should I go?” How do our muscles respond to spaceflight stressors long after we return to Earth?

Ghiarone, T., & Silva, K. A. S. (2026) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00225.2026

The role of ginsenosides in obesity-associated sarcopenia: Focus on E3 ubiquitin ligase-mediated regulation of protein homeostasis

Zhou, W., Li, P.-T., Li, H.-Y., & Li, W. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.179200

UBE2S promotes 5-fluorouracil resistance in colorectal cancer by activating non-canonical NF-κB/TYMS/TK1 signalingPreprint

Chu, C.-Y., Chou, C.-C., Liu, E.-H., Huang, T., Lee, Y.-C., Lee, Y.-L., Liu, C., Ho, K., Chen, K., Lee, K., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9241436/v1

Effects of Electrical Muscle Stimulation on Skeletal Muscle During Lipopolysaccharide-Induced Inflammation: A Controlled Murine Study

Matsukawa, S., Kai, S., Seo, H., & Egi, M. (2026) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000008260

Imeglimin provides dual hepatic and skeletal muscle protection in experimental MASH-associated sarcopenia

Osaki, Y., Kaji, K., Nishimura, N., Iwata, T., Kachi, H., Motokawa, Y., Mori, H., Shibamoto, A., Iwai, S., Tsuji, Y., et al. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168468

Integrated Multi-Omics Analysis Reveals Molecular Signatures Associated with Growth Divergence in Mandarin Fish (Siniperca chuatsi)

Ahamba, I. S., Kinkpe, L., Zhang, X., Yao, X., Ekugba, U. C., Hu, H., & Cui, R. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27198578

Role of the Ubiquitin-Proteasome Pathway in Skeletal Muscle

Kitajima, Y., & Suzuki, N. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_2 · Cited by 1

The ubiquitin proteasome system in atrophying skeletal muscle: roles and regulation

Bilodeau, P., Coyne, E. S., & Wing, S. S. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00125.2016 · Cited by 188

Dynamics and Interplay between Autophagy and Ubiquitin-proteasome system Coordination in Skeletal Muscle Atrophy

Singh, A. P., Yadav, A., Phogat, J., & Dabur, R. (2021) · Current Molecular Pharmacology · doi:10.2174/1874467214666210806163851 · Cited by 26

Regulation and involvement of the ubiquitin ligases in muscle atrophy

Sandri, M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.833 · Cited by 3

The dependency of autophagy and ubiquitin proteasome system during skeletal muscle atrophy

Singh, A. P., Phogat, J., Yadav, A., & Dabur, R. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00789-7 · Cited by 58