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Cited by 761

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A 26 S protease subunit that binds ubiquitin conjugates.

Open access
Deveraux, Q., Ustrell, V., Pickart, C., Rechsteiner, M.·1994·Journal of Biological Chemistry

Abstract

Ubiquitin-mediated proteolysis provides an important mechanism for regulating a variety of cellular processes. Ubiquitin-conjugated proteins are degraded by a 26 S protease that contains more than 30 different subunits. Of these, a single 50-kDa polypeptide, subunit 5, specifically binds ubiquitin-lysozyme conjugates. Binding is inhibited by short polymeric chains of ubiquitin but not by ubiquitin monomers or by lysozyme. In addition, subunit 5 binds free ubiquitin chains with efficient association requiring at least four ubiquitins. Thus, proteins conjugated to polymers of ubiquitin may be selected for degradation by a single subunit of the 26 S protease complex.

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Metadata

Authors
Deveraux, Q., Ustrell, V., Pickart, C., & Rechsteiner, M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-03
Volume
269
Issue
10
Pages
7059-7061
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1496897161
Cited by
761
References
1
FWCI
13.11
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: A 26 S protease subunit that binds ubiquitin conjugates. https://app.cochat.ai/papers/10.1016/s0021-9258(17)37244-7
The paper
Deveraux, Q., Ustrell, V., Pickart, C., & Rechsteiner, M. (1994). A 26 S protease subunit that binds ubiquitin conjugates. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)37244-7

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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.