Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy

By S. Bodine, E. Latres, S. Baumhueter, Venus Lai, L. Nuñez, B. A. Clarke, W. Poueymirou, Frank J. Panaro, Erqian Na, K. Dharmarajan and 6 more. Science, 2001

3,522 citations recorded by the source corpus.

Subfields: Cardiology and Cardiovascular Medicine, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/51a1b423937405c59e33e9946ce225bb20cad14c

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In Cardiology and Cardiovascular Medicine

1. S. Schiaffino
2. C. Mammucari
3. A. Goldberg
4. M. Birnbaum
5. A. V. D. Heuvel
6. David H. Gross
7. C. Gregorio
8. K. Clark

In Genetics

1. M. Sandri
2. A. Goldberg
3. D. Glass
4. P. Delafontaine
5. P. Bonaldo
6. J. Hawley
7. Vernon G. Coffey
8. D. G. Gibson

In Molecular Biology

1. M. Sandri
2. S. Schiaffino
3. A. Goldberg
4. C. Mammucari
5. D. Glass
6. S. Lecker
7. E. Masiero
8. J. Sacheck

Citations in the corpus

• TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases (2005, background): “In contrast, when the Murf1 null mice are challenged in the same atrophy model, they show a significant muscle sparing compared to wild-type controls, very likely due to impairment of proteasome-mediated degradation of some muscle proteins.((29))”
• FoxO3 controls autophagy in skeletal muscle in vivo. (2007, background): “Importantly , the rate of muscle atrophy is markedly reduced by targeted inactivation of these genes (Bodine et al., 2001a).”
• A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy (2012, neutral): “Small effects were also observed in the expression of the atrophy-related genesMuRF-1 and atrogin-1/MAFbx (Figure 3D) (Bodine et al., 2001; Gomes et al., 2001).”
• Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models (2011, background): “Their role in muscle-mass regulation is supported by the finding that muscle atrophy induced by denervation is partially prevented in both MuRF1 null and atrogin1/MAFbx null mice [ 92 ].”
• During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation (2009, background): “As reported previously (Bodine et al., 2001), these muscles in the WT lost 35% of their mass, but only 20% in the MuRF1 (P < 0.”
• Glucocorticoid-induced skeletal muscle atrophy. (2013, background): “…ubiquitin of the protein to be degraded (ubiquitin; 14 kDa E2, a conjugating enzyme: Atrogin-1 and MuRF-1, two muscle-specific E3 ubiquitin ligases (Bodine et al., 2001)) or directly responsible for the protein degradation by the proteasome (several subunits of the 20S proteasome) (Mitch and…”