The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Ubiquitin modifications
Open accessAbstract
Protein ubiquitination is a dynamic multifaceted post-translational modification involved in nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid protein ubiquitin is subjected to further modifications, creating a multitude of distinct signals with distinct cellular outcomes, referred to as the 'ubiquitin code'. Ubiquitin can be ubiquitinated on seven lysine (Lys) residues or on the N-terminus, leading to polyubiquitin chains that can encompass complex topologies. Alternatively or in addition, ubiquitin Lys residues can be modified by ubiquitin-like molecules (such as SUMO or NEDD8). Finally, ubiquitin can also be acetylated on Lys, or phosphorylated on Ser, Thr or Tyr residues, and each modification has the potential to dramatically alter the signaling outcome. While the number of distinctly modified ubiquitin species in cells is mind-boggling, much progress has been made to characterize the roles of distinct ubiquitin modifications, and many enzymes and receptors have been identified that create, recognize or remove these ubiquitin modifications. We here provide an overview of the various ubiquitin modifications present in cells, and highlight recent progress on ubiquitin chain biology. We then discuss the recent findings in the field of ubiquitin acetylation and phosphorylation, with a focus on Ser65-phosphorylation and its role in mitophagy and Parkin activation.
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Cites
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A guide to antigen processing and presentation
Pishesha, N., Harmand, T. J., & Ploegh, H. L. (2022) · Nature Reviews Immunology · doi:10.1038/s41577-022-00707-2 · Cited by 805
Specificity, versatility, and control of TGF-β family signaling
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The role of ubiquitination in tumorigenesis and targeted drug discovery
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A comprehensive compilation of SUMO proteomics
Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514
A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment
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Metadata
- Authors
- Swatek, K. N., & Komander, D.
- Venue
- Cell Research
- Published
- 2016-03-25
- Volume
- 26
- Issue
- 4
- Pages
- 399-422
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- OpenAlex
- W4210757594
- Cited by
- 2,081
- References
- 27
- FWCI
- 51.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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