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- W2125362863 endingPage "244" @default.
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- W2125362863 abstract "Viruses interact with the host ubiquitination system in a variety of ways. Viral proteins are often a substrate for ubiquitination, which leads to proteasomal degradation. Viruses also have functions to modify the cellular ubiquitination machinery. Recently, deubiquitinating protease (DUB) activity has been found in many viral proteins. In herpesviruses, the DUB domain is found within the large tegument protein, which is conserved in all members of the herpesvirus family. Although a limited number of viral and cellular targets have been identified to date, accumulating evidence shows that herpesviral DUBs may primarily target key cellular regulators of immune signaling pathways to promote viral replication. In this review, we summarize the recent findings on viral DUBs. In particular, we focus on the herpesviral DUBs and their targets, and discuss their potential roles in the regulation of immune signaling pathways." @default.
- W2125362863 created "2016-06-24" @default.
- W2125362863 creator A5028291984 @default.
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- W2125362863 date "2013-01-01" @default.
- W2125362863 modified "2023-10-16" @default.
- W2125362863 title "Herpesvirus-encoded Deubiquitinating Proteases and Their Roles in Regulating Immune Signaling Pathways" @default.
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- W2125362863 doi "https://doi.org/10.4167/jbv.2013.43.4.244" @default.
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