Journal
BIOLOGICAL CHEMISTRY
Volume 387, Issue 7, Pages 853-862Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2006.106
Keywords
adenovirus protease; herpesvirus UL36 tegument protein; protein structure comparison; SARS coronavirus papain-like protease; ubiquitin; ubiquitin-like modifiers
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Protein ubiquitination has been identified as a regulatory mechanism in key cellular activities, and deubiquitination is recognized as an important step in processes governed by ubiquitin and ubiquitin-like modifiers. Viruses are known to target ubiquitin and ubiquitin-like modifier pathways using various strategies, including the recruitment of host deubiquitinating enzymes. Deubiquitinating activities have recently been described for proteins from three different virus families (adenovirus, coronavirus and herpesvirus), and predicted for others. This review centers on structural-functional aspects that characterize the confirmed viral deubiquitinating enzymes, and their relationships to established families of cellular deubiquitinating enzymes.
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