Extended ubiquitin species are protein-based DUB inhibitors-Reference-Cited by-同舟云学术

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Extended ubiquitin species are protein-based DUB inhibitors

Published:2014-07-06 Issue:8 Volume:10 Page:664-670
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Krutauz Daria,Reis Noa,Nakasone Mark A,Siman Peter,Zhang Daoning,Kirkpatrick Donald S,Gygi Steven P,Brik Ashraf,Fushman David,Glickman Michael H

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.1574.pdf

Reference57 articles.

1. Glickman, M.H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373–428 (2002).

2. Finley, D., Ulrich, H.D., Sommer, T. & Kaiser, P. The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics 192, 319–360 (2012).

3. Komander, D. Mechanism, specificity and structure of the deubiquitinases. Subcell. Biochem. 54, 69–87 (2010).

4. Lee, M.J., Lee, B.H., Hanna, J., King, R.W. & Finley, D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell. Proteomics 10, R110.003871 (2011).

5. Guterman, A. & Glickman, M.H. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J. Biol. Chem. 279, 1729–1738 (2004).

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