The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.
Open accessAbstract
The ubiquitin-proteasome proteolytic pathway has recently been reported to be of major importance in the breakdown of skeletal muscle proteins.The first step in this pathway is the cova- lent attachment of polyubiquitin chains to the targeted protein.Polyubiquitylated proteins are then recognized and degraded by the 26S proteasome complex.In this review, we critically analyse recent findings in the regulation of this pathway, both in animal models of muscle wasting and in some human diseases.The identification of regulatory steps of ubiquitin conjugation to protein substrates and/or of the proteolytic activities of the proteasome should lead to new concepts that can be used to manipulate muscle protein mass.Such concepts are essential for the devel- opment of anti-cachectic therapies for many clinical situations.@ Inra/Elsevier, Paris skeletal muscle / protein breakdown / ubiquitin / proteasome Résumé -Protéolyse musculaire ubiquitine-protéasome dépendante.Il a été récemmment démontré que la protéolyse ubiquitine-protéasome dépendante joue un rôle majeur dans la dégradation des protéines musculaires.La première étape de cette voie protéolytique correspond à la fixation covalente de chaînes polyubiquitylées sur les substrats protéiques.Ces protéines polyubiquitylées sont ultérieurement spécifiquement reconnues et dégradées par le protéasome 26S.Les derniers progrès accomplis dans la compréhension de la régulation de ce système dans les modèles animaux de fontes protéiques musculaires, et dans certaines situations cliniques, sont ana- lysés de façon critique dans cette revue bibliographique.L'identification d'étapes régulatrices de 1'ubiquitylation des substrats protéiques, et/ou des activités protéolytiques du protéasome, devrait conduire à de nouveaux concepts utilisables pour manipuler le dépôt des protéines musculaires.En particulier, ces concepts sont indispensables au développement de traitements anti-cachectiques dans de nombreuses situations cliniques.
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“Especially in muscle, proteolysis by the UPS is a major mechanism involved in myofibrillar protein degradation (Attaix et al., 1998; Hasselgren et al., 2002).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Attaix et al., 1998
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STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438
The Proteasome: Paradigm of a Self-Compartmentalizing Protease
Baumeister, W. P., Walz, J., Zühl, F., & Seemüller, E. (1998) · Cell · doi:10.1016/s0092-8674(00)80929-0 · Cited by 1,497
THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION
Hershko, A., & Ciechanover, A. J. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.003553 · Cited by 1,448
Protein turnover in mammalian tissues and in the whole body
Waterlow, J. C., Garlick, P. J., & Millward, D. J. (1978) · Medical Entomology and Zoology · Cited by 1,227
Mechanisms of Muscle Wasting — The Role of the Ubiquitin–Proteasome Pathway
Mitch, W. E., & Goldberg, A. L. (1996) · New England Journal of Medicine · doi:10.1056/nejm199612193352507 · Cited by 1,163
A 26 S protease subunit that binds ubiquitin conjugates.
Deveraux, Q. L., Ustrell, V., Pickart, C. M., & Rechsteiner, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37244-7 · Cited by 765
Bailey, J. L., Wang, X., England, B. K., Price, S. R., Ding, X., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118566 · Cited by 455
Tsujinaka, T., Fujita, J., Ebisui, C., Yano, M., Kominami, E., Suzuki, K., Tanaka, K., Katsume, A., Ohsugi, Y., Shiozaki, H., et al. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118398 · Cited by 421
Mitch, W. E., Medina, R., Grieber, S., May, R. C., England, B. K., Price, S. R., Bailey, J. L., & Goldberg, A. L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117208 · Cited by 405
Price, S. R., Bailey, J. L., Wang, X., Jurkovitz, C. T., England, B. K., Ding, X., Phillips, L. S., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118968 · Cited by 348
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Proteolytic and lipolytic responses to starvation
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Metadata
- Authors
- Attaix, D., Aurousseau, E., Combaret, L., Kee, A., Larbaud, D., Rallière, C., Souweine, B., Taillandier, D., & Tilignac, T.
- Affiliations
- Centre de Recherche en Nutrition Humaine d'Auvergne (FR)
- Venue
- Reproduction Nutrition Development
- Publisher
- EDP Sciences
- Published
- 1998
- Volume
- 38
- Issue
- 2
- Pages
- 153-165
- ISSN
- 0003-388X (ISSN-L)
- 0926-5287
- OpenAlex
- W2102589258
- Cited by
- 109
- References
- 50
- Citations by year
- 2025: 1 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 1 · 2018: 3 · 2017: 2 · 2015: 1 · 2014: 2 · 2013: 4 · 2012: 3
- FWCI
- 0.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- annales de biologie animale biochimie biophysique (publishedVersion)
- PubMed (publishedVersion)
- Springer Link (Chiba Institute of Technology) (submittedVersion)
- HAL (submittedVersion, other-oa)
- HAL (submittedVersion)
- Funders
- Institut National de la Recherche Agronomique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- ubiquitin-proteasome system, skeletal muscle protein degradation, polyubiquitination, 26S proteasome, muscle atrophy, cachexia
- MeSH terms
- Animals, Cysteine Endopeptidases, Humans, Multienzyme Complexes, Muscle Proteins, Endopeptidases, Ubiquitins, Muscle, Skeletal, Proteasome Endopeptidase Complex
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