Ubiquitination: RING for destruction?
Open accessAbstract
Ubiquitination targets proteins for degradation and is a potent regulator of cellular protein function. Recent results implicate the RING finger domain in specific ubiquitination events; it is possible that all RING proteins act as E3 ubiquitin protein ligases, with implications for a variety of biological areas.
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It has been suggested that all RING-finger proteins are E3-Ub ligases.
“it has been suggested that all RINGfinger proteins are E3-Ub ligases”
From Limb-Girdle Muscular Dystrophy Type 2H Associated with Mutation in TRIM32, a Putative E3-Ubiquitin–Ligase Gene (2002) · cites this paper as Freemont 2000
Cites
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Does this have a familiar RING?
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- Authors
- Freemont, P. S.
- Corresponding author
- Freemont, Paul S.
- ORCID
- Freemont, Paul S.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 10
- Issue
- 2
- Pages
- R84-R87
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2088619528
- Cited by
- 522
- References
- 20
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 20 · 2023: 5 · 2022: 8 · 2021: 11 · 2020: 7 · 2019: 16 · 2018: 9 · 2017: 11 · 2016: 7 · 2015: 10 · 2014: 11 · 2013: 7 · 2012: 15
- FWCI
- 22.38
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- ubiquitination, RING domain, E3 ubiquitin ligase, protein degradation, protein function regulation
- MeSH terms
- Amino Acid Sequence, Proteins, Ubiquitins, Amino Acid Motifs
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