The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin.
Open accessAbstract
Previous studies have indicated that the ATP-dependent 26S protease complex that degrades proteins conjugated to ubiquitin is formed by the assembly of three factors in an ATP-requiring process. We now identify one of the factors as the 20S "multicatalytic" protease, a complex of low molecular weight subunits widely distributed in eukaryotic cells. Comparison of the subunit compositions of purified 20S and 26S complexes indicates that the former is an integral part of the latter. By the use of detergent treatment to activate latent protease activity, we show that the 20S protease becomes incorporated into the 26S complex in the ATP-dependent assembly process. It thus seems that the 20S protease is the "catalytic core" of the 26S complex of the ubiquitin proteolytic pathway.
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Citations
Cites
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
Cited by
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Self-citationPalombella, V. J., Rando, O. J., Goldberg, A. L., & Maniatis, T. (1994) · Cell · doi:10.1016/s0092-8674(94)90482-0 · Cited by 2,096
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
Proteolysis: from the lysosome to ubiquitin and the proteasome
Ciechanover, A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1552 · Cited by 1,133
Huibregtse, J. M., Scheffner, M., & Howley, P. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04990.x · Cited by 879
Metadata
- Authors
- Eytan, E., Ganoth, D., Armon, T., & Hershko, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1989-10
- Volume
- 86
- Issue
- 20
- Pages
- 7751-7755
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1995596496
- Cited by
- 365
- References
- 1
- FWCI
- 9.55
- Type
- journal article
- Language
- en
- Open access
- green
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- Eytan, E., Ganoth, D., Armon, T., & Hershko, A. (1989). ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.20.7751
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
