Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy

By Marcelo Gomes, S. Lecker, R. Jagoe, A. Navon, A. Goldberg. Proceedings of the National Academy of Sciences of the United States of America, 2001

1,808 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2167ce152521c3e462db3aaaf1b4002c4c270d55

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. M. Sandri
2. A. Goldberg
3. D. Glass
4. J. Hawley
5. Vernon G. Coffey
6. S. Schiaffino
7. S. Lecker
8. J. Sacheck

In Molecular Biology

1. M. Sandri
2. A. Goldberg
3. S. Schiaffino
4. D. Glass
5. C. Mammucari
6. J. Hawley
7. Vernon G. Coffey
8. S. Lecker

Citations in the corpus

• FoxO3 controls autophagy in skeletal muscle in vivo. (2007, background): “The activity of this pathway is markedly increased in atrophying muscle due to transcriptional activation of ubiquitin; several proteasomal subunit genes; and two muscle-specific ubiquitin ligases, atrogin-1/ MAFbx andMuRF1, which are induced severalfold during early stages of muscle atrophy (Gomes ”
• The calpain system. (2003, methodology): “A similar microarray assay independently found that expression of MuRF1 was upregulated in fasting, ureminc, and diabetic mice (140).”
• IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. (2004, methodology): “Recently, we identified a number of parallel changes in gene expression that are common to these different forms of muscle atrophy (termed atrophy-related genes or “atrogenes”) (15, 23); yet it is unclear how these various transcriptional changes during atrophy are coordinately induced.”
• Systematic analysis and nomenclature of mammalian F-box proteins. (2004, positive): “FBXO32 is up-regulated during muscle atrophy (Bodine et al. 2001; Gomes et al. 2001).”
• The molecular basis of skeletal muscle atrophy. (2004, background): “MAFbx and found it to be markedly upregulated with atrophy resulting from disuse (9) and also in cachexia (29).”
• Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival. (2010, background): “In the atrophying muscles, multiple components of this pathway are induced, including the muscle-specific E3 ligases, Atrogin-1 and MuRF1, and their induction is essential in rapid atrophy (Bodine et al., 2001; Gomes et al., 2001).”
• Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases (2007, methodology): “A plasmid-based mouse skeletal muscle cDNA library was used as the PCR template as described previously (3).”
• 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): “Direct evidence for FoxO-dependent activation of the ubiquitin-proteasome pathway was obtained with the demonstration that the muscle-specific ubiquitin ligases atrogin-1/MAFbx and MuRF1, which are induced in various models of muscle atrophy [92, 93 ], are transcriptional targets of FoxO factors, an”
• Cancer cachexia: mediators, signaling, and metabolic pathways. (2012, background): “MAFbx/Atrogin-1 also serves as a high-fidelity marker of acute muscle atrophy, being upregulated in multiple settings of cachexia (Gomes et al., 2001), in addition to immobi-”