The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Polyubiquitin chains: functions, structures, and mechanisms
Open accessAbstract
Abstract.Ubiquitin is a highly conserved 76-aminoacid polypeptide that is found throughout the eukaryotic kingdom. The covalent conjugation of ubiquitin (often in the form of a polymer) to substrates governs a variety of biological processes ranging from proteolysis to DNA damage tolerance. The functional flexibility of this post-translational modification has its roots in the existence of a large number of ubiquitinating enzymes that catalyze the formation of distinct ubiquitin polymers, which in turn encode different signals. This review summarizes recent advances in the field with an emphasis on the non-canonical functions of polyubiquitination. We also discuss the potential mechanism of chain linkage specification as well as how structural disparity in ubiquitin polymers may be distinguished by ubiquitin receptors to translate the versatile ubiquitin signals into various cellular functions.
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Self-citationCdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
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Self-citationAutophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
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The fine-tuning of proteolytic pathways in Alzheimer’s disease
Cecarini, V., Bonfili, L., Cuccioloni, M., Mozzicafreddo, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2238-6 · Cited by 21
Metadata
- Authors
- Li, W., & Ye, Y.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2008-04-26
- Volume
- 65
- Issue
- 15
- Pages
- 2397-2406
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- OpenAlex
- W2036051377
- Cited by
- 270
- References
- 8
- FWCI
- 7.20
- Type
- journal article
- Language
- en
- Open access
- green
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