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Wiley, Protein Science, 4(23), p. 344-353, 2014

DOI: 10.1002/pro.2415

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Mechanisms for regulating deubiquitinating enzymes

Journal article published in 2014 by Cynthia Wolberger ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes, which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate deubiquitinating enzyme activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which deubiquitinating enzyme activity and specificity is regulated.