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Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms
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Auto-ubiquitination can be antagonized by deubiquitinating enzymes, which remove ubiquitin from the E3.
“Auto-ubiquitination can be antagonized by deubiquitinating enzymes (DUBs), which remove Ub from the E3 (de Bie & Ciechanover, 2011).”
From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as de Bie & Ciechanover, 2011
Functional coupling of target ubiquitylation and degradation to that of the cognate E3-ubiquitin ligase is an emerging concept in the ubiquitin field.
“Functional coupling of target ubiquitylation and degradation to that of the cognate E3-ubiquitin ligase is an emerging concept in the ubiquitin fi eld ( 53 ).”
From The LXR-IDOL axis defines a clathrin-, caveolae-, and dynamin-independent endocytic route for LDLR internalization and lysosomal degradation (2013) · cites this paper as [53]
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RING Domain E3 Ubiquitin Ligases
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Okamoto, K., Taya, Y., & Nakagama, H. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.021 · Cited by 76
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Metadata
- Authors
- de Bie, P., & Ciechanover, A.
- Venue
- Cell Death & Differentiation
- Published
- 2011-03-04
- Volume
- 18
- Issue
- 9
- Pages
- 1393-1402
- ISSN
- 1350-9047
- 1476-5403
- Cited by
- 296
- References
- 4
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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