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Cited by 611

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination

Open access
Metzger, Meredith B., Pruneda, Jonathan N., Klevit, Rachel E., Weissman, Allan M.·2014·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Abstract

RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated in numerous cellular processes. In part because of their importance in human physiology and disease, these proteins and their cellular functions represent an intense area of study. Here we review recent advances in RING-type E3 recognition of substrates, their cellular regulation, and their varied architecture. Additionally, recent structural insights into RING-type E3 function, with a focus on important interactions with E2s and ubiquitin, are reviewed. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System.

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Metadata

Authors
Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M.
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2014-01
Volume
1843
Issue
1
Pages
47-60
ISSN
0167-4889 (ISSN-L)
OpenAlex
W1973921769
Cited by
611
References
8
FWCI
13.72
Type
journal article
Language
en
Open access
bronze

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Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M. (2014). RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2013.05.026

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.