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Cited by 2,487

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STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES

Coux, Olivier, Tanaka, Keiji, Goldberg, Alfred L.·1996·Annual Review of Biochemistry

Abstract

The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20S (700-kDa) proteasome contains multiple peptidase activities that function through a new type of proteolytic mechanism involving a threonine active site. The 26S (2000-kDa) complex, which degrades ubiquitinated proteins, contains in addition to the 20S proteasome a 19S regulatory complex composed of multiple ATPases and components necessary for binding protein substrates. The proteasome has been highly conserved during eukaryotic evolution, and simpler forms are even found in archaebacteria and eubacteria. Major advances have been achieved recently in our knowledge about the molecular organization of the 20S and 19S particles, their subunits, the proteasome’s role in MHC-class 1 antigen presentation, and regulators of its activities. This article focuses on recent progress concerning the biochemical mechanisms and intracellular functions of the 20S and 26S proteasomes.

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Metadata

Authors
Coux, O., Tanaka, K., & Goldberg, A. L.
Venue
Annual Review of Biochemistry
Published
1996-06
Volume
65
Issue
1
Pages
801-847
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2178503716
Cited by
2,487
References
0
FWCI
60.98
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES. https://app.cochat.ai/papers/10.1146/annurev.bi.65.070196.004101
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Coux, O., Tanaka, K., & Goldberg, A. L. (1996). STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.bi.65.070196.004101

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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.