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Cited by 730

The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.

TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases

Meroni, Germana, Diez‐Roux, Graciana·2005·BioEssays

Abstract

The TRIM/RBCC proteins are defined by the presence of the tripartite motif composed of a RING domain, one or two B‐box motifs and a coiled‐coil region. These proteins are involved in a plethora of cellular processes such as apoptosis, cell cycle regulation and viral response. Consistently, their alteration results in many diverse pathological conditions. The highly conserved modular structure of these proteins suggests that a common biochemical function may underlie their assorted cellular roles. Here, we review recent data indicating that some TRIM/RBCC proteins are implicated in ubiquitination and propose that this large protein family represents a novel class of ‘single protein RING finger’ ubiquitin E3 ligases. BioEssays 27:1147–1157, 2005. © 2005 Wiley Periodicals, Inc.

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Metadata

Authors
Meroni, G., & Diez‐Roux, G.
Venue
BioEssays
Publisher
Wiley
Published
2005-10-19
Volume
27
Issue
11
Pages
1147-1157
ISSN
  • 0265-9247 (ISSN-L)
  • 1521-1878
OpenAlex
W2131037087
Cited by
730
References
104
FWCI
1.26
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases. https://app.cochat.ai/papers/10.1002/bies.20304
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Meroni, G., & Diez‐Roux, G. (2005). TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases. BioEssays. https://doi.org/10.1002/bies.20304

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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.