The DOI matches its Crossref record; 145 of the 145 references it cites were found in a registry or an index.
The ubiquitin–proteasome system in regulation of the skeletal muscle homeostasis and atrophy: from basic science to disorders
Open accessAbstract
Skeletal muscle is one of the most abundant and highly plastic tissues. The ubiquitin-proteasome system (UPS) is recognised as a major intracellular protein degradation system, and its function is important for muscle homeostasis and health. Although UPS plays an essential role in protein degradation during muscle atrophy, leading to the loss of muscle mass and strength, its deficit negatively impacts muscle homeostasis and leads to the occurrence of several pathological phenotypes. A growing number of studies have linked UPS impairment not only to matured muscle fibre degeneration and weakness, but also to muscle stem cells and deficiency in regeneration. Emerging evidence suggests possible links between abnormal UPS regulation and several types of muscle diseases. Therefore, understanding of the role of UPS in skeletal muscle may provide novel therapeutic insights to counteract muscle wasting, and various muscle diseases. In this review, we focussed on the role of proteasomes in skeletal muscle and its regeneration, including a brief explanation of the structure of proteasomes. In addition, we summarised the recent findings on several diseases and elaborated on how the UPS is related to their pathological states.
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“The ubiquitin–proteasome system plays a major role in protein content turnover by degrading misfolded or defective proteins [163,164].”
From Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting (2023) · cites this paper as [163]
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2 retracted
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Mitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies
Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 134
Metadata
- Authors
- Kitajima, Y., Yoshioka, K., & Suzuki, N.
- Affiliations
- Institute of Molecular Embryology and Genetics, Kumamoto University (JP)
- Tohoku University (JP)
- Corresponding author
- Kitajima, Yasuo
- Suzuki, Naoki
- Venue
- The Journal of Physiological Sciences
- Publisher
- Elsevier BV
- Published
- 2020
- Volume
- 70
- Issue
- 1
- Pages
- 40
- ISSN
- 1880-6546 (ISSN-L)
- PMC
- PMC10717345
- OpenAlex
- W3085918938
- Cited by
- 171
- References
- 145
- Citations by year
- 2026: 28 · 2025: 43 · 2024: 33 · 2023: 25 · 2022: 30 · 2021: 12
- FWCI
- 1.60
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- The Journal of Physiological Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Takeda Science Foundation
- Grant-in-Aid for Scientific Research KAKENHI (15H05667, 16H05318, 18K07519, 18K17857, 20H04078)
- Suzuken Memorial Foundation (YK)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- ubiquitin-proteasome system, skeletal muscle homeostasis, muscle atrophy, proteasome, muscle regeneration, muscle stem cells, muscle fiber degeneration, myopathy, protein degradation
- MeSH terms
- Animals, Homeostasis, Humans, Muscle Proteins, Muscular Atrophy, Regeneration, Muscle, Skeletal, Muscle Development, Ubiquitin, Satellite Cells, Skeletal Muscle, Proteasome Endopeptidase Complex, Ubiquitination, Proteolysis
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