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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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Förster, Friedrich1, Autor           
Unverdorben, Pia1, Autor           
Sledz, Pawel2, Autor           
Baumeister, Wolfgang2, Autor           
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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Schlagwörter: UBIQUITINATED PROTEINS ACTIVATE; ATP-FUELED MACHINES; INITIATION-FACTOR 3; REGULATORY PARTICLE; 20S PROTEASOME; THERMOPLASMA-ACIDOPHILUM; DEUBIQUITINATING ENZYME; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; MOLECULAR ARCHITECTURE
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2013-09-03
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000330268600011
DOI: 10.1016/j.str.2013.08.010
 Art des Abschluß: -

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Titel: STRUCTURE
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Seiten: - Band / Heft: 21 (9) Artikelnummer: - Start- / Endseite: 1551 - 1562 Identifikator: ISSN: 0969-2126