Cited by 522Ubiquitin and proteasome pathwaysProtein Degradation and InhibitorsNF-κB Signaling Pathways

Ubiquitination: RING for destruction?

Open access
Freemont, Paul S.·2000·Current Biology

Abstract

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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Crossref · 10.1016/s0960-9822(00)00287-6

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Authors
Freemont, P. S.
Corresponding author
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
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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