The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Immunity by ubiquitylation: a reversible process of modification
Open accessAbstract
The conjugation of ubiquitin, a 76-amino-acid peptide, to a protein substrate provides a tag that either marks the labelled protein for degradation or modulates its function. The process of protein ubiquitylation — which is catalysed by coordinated enzymatic reactions that are mediated by enzymes known as E1, E2 and E3 — has an important role in the modulation of immune responses. Importantly, protein ubiquitylation is a reversible process, and removal of ubiquitin molecules is mediated by de-ubiquitylating enzymes: for example, A20, which has been implicated in the regulation of immune responses. In addition, the conjugation of ubiquitin-like molecules, such as ISG15 (interferon-stimulated protein of 15 kDa), to proteins is also involved in immune regulation. This Review covers recent progress in our understanding of protein ubiquitylation in the immune system.
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Cites
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Cited by
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The tumour suppressor CYLD is a negative regulator of RIG‐I‐mediated antiviral response
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The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon
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Metadata
- Authors
- Liu, Y.-C., Penninger, J., & Karin, M.
- Venue
- Nature Reviews Immunology
- Published
- 2005-12-01
- Volume
- 5
- Issue
- 12
- Pages
- 941-952
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- OpenAlex
- W1986706236
- Cited by
- 257
- References
- 11
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- bronze
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