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Cited by 1,242

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

SCF and Cullin/RING H2-Based Ubiquitin Ligases

Deshaies, R. J.·1999·Annual Review of Cell and Developmental Biology

Abstract

▪ Abstract Protein degradation is deployed to modulate the steady-state abundance of proteins and to switch cellular regulatory circuits from one state to another by abrupt elimination of control proteins. In eukaryotes, the bulk of the protein degradation that occurs in the cytoplasm and nucleus is carried out by the 26S proteasome. In turn, most proteins are thought to be targeted to the 26S proteasome by covalent attachment of a multiubiquitin chain. Ubiquitination of proteins requires a multienzyme system. A key component of ubiquitination pathways, the ubiquitin ligase, controls both the specificity and timing of substrate ubiquitination. This review is focused on a conserved ubiquitin ligase complex known as SCF that plays a key role in marking a variety of regulatory proteins for destruction by the 26S proteasome.

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Metadata

Authors
Deshaies, R. J.
Venue
Annual Review of Cell and Developmental Biology
Published
1999-11
Volume
15
Issue
1
Pages
435-467
ISSN
  • 1081-0706 (ISSN-L)
  • 1530-8995
OpenAlex
W2170634115
Cited by
1,242
References
2
FWCI
5.39
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: SCF and Cullin/RING H2-Based Ubiquitin Ligases. https://app.cochat.ai/papers/10.1146/annurev.cellbio.15.1.435
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Deshaies, R. J. (1999). SCF and Cullin/RING H2-Based Ubiquitin Ligases. Annual Review of Cell and Developmental Biology. https://doi.org/10.1146/annurev.cellbio.15.1.435

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

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