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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 381, Issue 9-10


The Ubiquitin System and the N-End Rule Pathway

Alexander Varshavsky / Glenn Turner / Fangyong Du / Youming Xie
Published Online: 2005-07-05 | DOI: https://doi.org/10.1515/BC.2000.101


Eukaryotes contain a highly conserved multienzyme system which covalently links a small protein, ubiquitin, to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, an ATP-dependent protease. Pathways that involve ubiquitin play major roles in a huge variety of processes, including cell differentiation, cell cycle, and responses to stress. In this article we briefly review the design of the ubiquitin system, and describe two recent advances, the finding that ubiquitin ligases interact with specific components of the 26S proteasome, and the demonstration that peptides accelerate their uptake into cells by activating the N-end rule pathway, one of several proteolytic pathways of the ubiquitin system.

About the article

Published Online: 2005-07-05

Published in Print: 2000-09-13

Citation Information: Biological Chemistry, Volume 381, Issue 9-10, Pages 779–789, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.101.

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