Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome-Reference-Cited by-同舟云学术

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Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome

Published:2015-08-24 Issue:9 Volume:22 Page:712-719
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Bashore Charlene,Dambacher Corey M,Goodall Ellen A,Matyskiela Mary E,Lander Gabriel C,Martin Andreas

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3075.pdf

Reference55 articles.

1. Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477–513 (2009).

2. Goldberg, A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895–899 (2003).

3. Goldberg, A.L. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans. 35, 12–17 (2007).

4. Verma, R. et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611–615 (2002).

5. Yao, T. & Cohen, R.E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403–407 (2002).

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