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- W4224254671 endingPage "4593" @default.
- W4224254671 startingPage "4593" @default.
- W4224254671 abstract "The ubiquitin system denotes a potent post-translational modification machinery that is capable of activation or deactivation of target proteins through reversible linkage of a single ubiquitin or ubiquitin chains. Ubiquitination regulates major cellular functions such as protein degradation, trafficking and signaling pathways, innate immune response, antiviral defense, and virus replication. The RNA sensor RIG-I ubiquitination is specifically induced by influenza A virus (IAV) to activate type I IFN production. Influenza virus modulates the activity of major antiviral proteins in the host cell to complete its full life cycle. Its structural and non-structural proteins, matrix proteins and the polymerase complex can regulate host immunity and antiviral response. The polymerase PB1-F2 of mutated 1918 IAV, adapts a novel IFN antagonist function by sending the DDX3 into proteasomal degradation. Ultimately the fate of virus is determined by the outcome of interplay between viral components and host antiviral proteins and ubiquitination has a central role in the encounter of virus and its host cell." @default.
- W4224254671 created "2022-04-26" @default.
- W4224254671 creator A5007375214 @default.
- W4224254671 creator A5013290027 @default.
- W4224254671 creator A5025005110 @default.
- W4224254671 creator A5067127764 @default.
- W4224254671 date "2022-04-21" @default.
- W4224254671 modified "2023-10-05" @default.
- W4224254671 title "The Roles of Ubiquitination in Pathogenesis of Influenza Virus Infection" @default.
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