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  Unveiling the Long-Held Secrets of the 26S Proteasome

Förster, F., Unverdorben, P., Sledz, P., & Baumeister, W. (2013). Unveiling the Long-Held Secrets of the 26S Proteasome. STRUCTURE, 21(9), 1551-1562. doi:10.1016/j.str.2013.08.010.

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 Creators:
Förster, Friedrich1, Author           
Unverdorben, Pia1, Author           
Sledz, Pawel2, Author           
Baumeister, Wolfgang2, Author           
Affiliations:
1Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: UBIQUITINATED PROTEINS ACTIVATE; ATP-FUELED MACHINES; INITIATION-FACTOR 3; REGULATORY PARTICLE; 20S PROTEASOME; THERMOPLASMA-ACIDOPHILUM; DEUBIQUITINATING ENZYME; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; MOLECULAR ARCHITECTURE
 Abstract: The 26S proteasome is a 2.5 MDa molecular machine for the degradation of substrates of the ubiquitin-proteasome pathway with a key role in cellular proteostasis. Until recently, only the structure of its core particle, the 20S proteasome, could be studied in detail, whereas the 19S regulatory particle or the holocomplex remained elusive. Novel integrative approaches have now revealed the molecular architecture of the entire complex and provided the first insights into the conformational changes during its functional cycle. Here we review the problems in structural studies of the 26S proteasome, the methods that made possible its structure determination, the architectural principles of the holocomplex, and its conformational space. These advances provide valuable insights into the mechanism of substrate recruitment and processing preceding their destruction in the 20S core particle.

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Language(s): eng - English
 Dates: 2013-09-03
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000330268600011
DOI: 10.1016/j.str.2013.08.010
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 21 (9) Sequence Number: - Start / End Page: 1551 - 1562 Identifier: ISSN: 0969-2126