Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2037114 | Cell | 2009 | 4 Pages |
Abstract
Assembly of complex structures such as the eukaryotic 26S proteasome requires intricate mechanisms that ensure precise subunit arrangements. Recent studies have shed light on the pathway for ordered assembly of the base of the 19S regulatory particle of the 26S proteasome by identifying new precursor complexes and four dedicated chaperones involved in its assembly.
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Authors
Henrike C. Besche, Andreas Peth, Alfred L. Goldberg,