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Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease
Open accessAbstract
Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape. The dysregulation of these mitochondrial proteins is linked to a range of human metabolic disorders. Perhaps most striking is that lipoylation itself, the proteins that add or remove the modification, as well as the proteins it decorates are all evolutionarily conserved from bacteria to humans, highlighting the importance of this essential cofactor. Here, we discuss the biological significance of protein lipoylation, the importance of understanding its regulation in health and disease states, and the advances in mass spectrometry-based proteomic technologies that can aid these studies.
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Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197
Cellular Fatty Acid Metabolism and Cancer
Currie, E., Schulze, A., Zechner, R., Walther, T. C., & Farese, R. V. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.05.017 · Cited by 2,123
Proteogenomics connects somatic mutations to signalling in breast cancer
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Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity
Mathias, R. A., Greco, T. M., Oberstein, A., Budayeva, H. G., Chakrabarti, R., Rowland, E. A., Kang, Y., Shenk, T., & Cristea, I. M. (2014) · Cell · doi:10.1016/j.cell.2014.11.046 · Cited by 430
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Cited by
Copper induces cell death by targeting lipoylated TCA cycle proteins
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Chen, L., Min, J., & Wang, F. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01229-y · Cited by 1,493
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Recent advances in molecular mechanisms of skin wound healing and its treatments
Mamun, A. A., Shao, C., Geng, P., Wang, S., & Xiao, J. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1395479 · Cited by 284
Chiral Posttranslational Modification to Lysine ε-Amino Groups
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Metadata
- Authors
- Rowland, E. A., Snowden, C. K., & Cristea, I. M.
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2018-02
- Volume
- 42
- Pages
- 76-85
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W2768844677
- Cited by
- 255
- References
- 4
- FWCI
- 0.30
- Type
- journal article
- Language
- en
- Open access
- bronze
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