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- W4313398575 abstract "Viral envelope glycoproteins are crucial for viral infections. In the process of enveloped viruses budding and release from the producer cells, viral envelope glycoproteins are presented on the viral membrane surface as spikes, promoting the virus's next-round infection of target cells. However, the host cells evolve counteracting mechanisms in the long-term virus-host co-evolutionary processes. For instance, the host cell antiviral factors could potently suppress viral replication by targeting their envelope glycoproteins through multiple channels, including their intracellular synthesis, glycosylation modification, assembly into virions, and binding to target cell receptors. Recently, a group of studies discovered that some host antiviral proteins specifically recognized host proprotein convertase (PC) furin and blocked its cleavage of viral envelope glycoproteins, thus impairing viral infectivity. Here, in this review, we briefly summarize several such host antiviral factors and analyze their roles in reducing furin cleavage of viral envelope glycoproteins, aiming at providing insights for future antiviral studies." @default.
- W4313398575 created "2023-01-06" @default.
- W4313398575 creator A5000696502 @default.
- W4313398575 creator A5008184670 @default.
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- W4313398575 creator A5057055806 @default.
- W4313398575 creator A5058560135 @default.
- W4313398575 creator A5062782692 @default.
- W4313398575 creator A5069771802 @default.
- W4313398575 date "2023-02-01" @default.
- W4313398575 modified "2023-10-11" @default.
- W4313398575 title "Host antiviral factors hijack furin to block SARS-CoV-2, ebola virus, and HIV-1 glycoproteins cleavage" @default.
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- W4313398575 doi "https://doi.org/10.1080/22221751.2022.2164742" @default.
- W4313398575 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36591809" @default.
- W4313398575 hasPublicationYear "2023" @default.
- W4313398575 type Work @default.