The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Regulation of muscle protein synthesis and the effects of catabolic states
Open accessAbstract
Protein synthesis and degradation are dynamically regulated processes that act in concert to control the accretion or loss of muscle mass. The present article focuses on the mechanisms involved in the impairment of protein synthesis that are associated with skeletal muscle atrophy. The vast majority of mechanisms known to regulate protein synthesis involve modulation of the initiation phase of mRNA translation, which comprises a series of reactions that result in the binding of initiator methionyl-tRNAi and mRNA to the 40S ribosomal subunit. The function of the proteins involved in both events has been shown to be repressed under atrophic conditions such as sepsis, cachexia, chronic kidney disease, sarcopenia, and disuse atrophy. The basis for the inhibition of protein synthesis under such conditions is likely to be multifactorial and includes insulin/insulin-like growth factor 1 resistance, pro-inflammatory cytokine expression, malnutrition, corticosteroids, and/or physical inactivity. The present article provides an overview of the existing literature regarding mechanisms and signaling pathways involved in the regulation of mRNA translation as they apply to skeletal muscle wasting, as well as the efficacy of potential clinical interventions such as nutrition and exercise in the maintenance of skeletal muscle protein synthesis under atrophic conditions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · cited 1×
“Instead, amino acids promote the assembly of a mTORC1 complex with the Rag small GTPases and a heteropentameric complex referred to as Ragulator at the late endosomal/lysosomal membrane (Sancak et al., 2010).”
BackgroundRheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367
The TSC1–TSC2 complex: a molecular switchboard controlling cell growth
Huang, J., & Manning, B. D. (2008) · Biochemical Journal · doi:10.1042/bj20080281 · Cited by 1,237 · cited 9×
“As noted above, impaired insulin and Akt signaling to mTORC1 may be a consequence of concomitant activation of AMPK.”
BackgroundInfluentialKatsanos, C. S., Kobayashi, H., Sheffield-Moore, M., Aarsland, A., & Wolfe, R. R. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00488.2005 · Cited by 923
Sebastián, D., Hernández-Alvarez, M. I., Segalés, J., Sorianello, E., Muñoz, J. P., Sala, D., Waget, A., Liesa, M., Paz, J. C., Gopalacharyulu, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108220109 · Cited by 673
Yang, H.-S., Jansen, A. P., Komar, A. A., Zheng, X., Merrick, W. C., Costes, S., Lockett, S. J., Sonenberg, N., & Colburn, N. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.26-37.2003 · Cited by 494
Amino acid ingestion improves muscle protein synthesis in the young and elderly
Paddon-Jones, D., Sheffield-Moore, M., Zhang, X.-J., Volpi, E., Wolf, S. E., Aarsland, A., Ferrando, A. A., & Wolfe, R. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00368.2003 · Cited by 467 · cited 6×
“However, the use of protein supplementation has yielded mixed results with some studies showing increased rates of protein synthesis in response to amino acid supplementation (Guillet et al., 2004; Paddon-Jones et al., 2006; Paddon-Jones et al., 2003) whereas others have not (Katsanos et al.”
BackgroundResultInfluentialDrummond, M. J., Fry, C. S., Glynn, E. L., Dreyer, H. C., Dhanani, S., Timmerman, K. L., Volpi, E., & Rasmussen, B. B. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.163816 · Cited by 439 · cited 2×
“The phosphorylation of 4E-BP1, as well as the increase in protein synthesis, that occurs in muscle in response to either consumption of amino acids (Dickinson et al., 2011) or resistance exercise (Drummond et al., 2009) is also blocked by rapamycin treatment.”
BackgroundMonocyte Cytokine Production in an Elderly Population: Effect of Age and Inflammation
Roubenoff, R., Harris, T. B., Abad, L. W., Wilson, P. W. F., Dallal, G. E., & Dinarello, C. A. (1998) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/53a.1.m20 · Cited by 418 · cited 2×
“Human data show significantly higher levels of circulating IL-6 and IL-6 receptor in old individuals (Roubenoff et al., 1998), with IL-6 levels being a significant predictor of sarcopenia (Payette et al.”
Background
Cited by
The Sick and the Weak: Neuropathies/Myopathies in the Critically Ill
Friedrich, O., Reid, M. B., Van den Berghe, G., Vanhorebeek, I., Hermans, G., Rich, M. M., & Larsson, L. (2015) · Physiological Reviews · doi:10.1152/physrev.00028.2014 · Cited by 396
Protein Consumption and the Elderly: What Is the Optimal Level of Intake?
Baum, J., Kim, I.-Y., & Wolfe, R. (2016) · Nutrients · doi:10.3390/nu8060359 · Cited by 312
Ribosome biogenesis: Emerging evidence for a central role in the regulation of skeletal muscle mass
Chaillou, T., Kirby, T. J., & McCarthy, J. J. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24604 · Cited by 211
The Hippo pathway effector YAP is a critical regulator of skeletal muscle fibre size
Watt, K. I., Turner, B. J., Hagg, A., Zhang, X., Davey, J. R., Qian, H., Beyer, C., Winbanks, C. E., Harvey, K. F., & Gregorevic, P. (2015) · Nature Communications · doi:10.1038/ncomms7048 · Cited by 164
Rivas, D. A., McDonald, D. J., Rice, N. P., Haran, P. H., Dolnikowski, G. G., & Fielding, R. A. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00198.2015 · Cited by 132
Metadata
- Authors
- Gordon, B. S., Kelleher, A. R., & Kimball, S. R.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 45
- Issue
- 10
- Pages
- 2147-2157
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W2029296519
- Cited by
- 208
- References
- 28
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Regulation of muscle protein synthesis and the effects of catabolic states. https://app.cochat.ai/papers/10.1016/j.biocel.2013.05.039
- The paper
- Gordon, B. S., Kelleher, A. R., & Kimball, S. R. (2013). Regulation of muscle protein synthesis and the effects of catabolic states. The International Journal of Biochemistry & Cell Biology. https://doi.org/10.1016/j.biocel.2013.05.039
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.