IndraLab

Statements

Nef inhibits USP15. 5 / 5
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"Further, while the amount of intracellular Nef and USP15 was mutually regulated, USP15 mediated degradation of Nef was stronger than Nef mediated USP15 degradation, implying that USP15 could be employed to knock out Nef, a molecule essential to pathogenicity, within HIV-1 infected cells."
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"These data indicate that Nef expressed from the wt-HIV-1-, but not from Deltanef-HIV-1-replicating cells, degraded USP15, lowering the amount of intracellular USP15, which in turn vitiated USP15 induced degradation of viral proteins and thereby HIV-1 replication, where Nef degrades USP15, but USP15 mediated Nef degradation is more potent (XREF_FIG)."
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"These data collectively demonstrated that stability of Nef and USP15 is regulated reciprocally, and that USP15 mediated degradation of Nef was more pronounced than Nef mediated degradation of USP15."
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"Further, Nef, but not Gag, degraded USP15, suggesting that reciprocal degradation of Nef and USP15 could play a central role in coordinating decay of viral proteins and hence HIV-1 replication, underlining the dynamic competition between the molecular determinants of the infecting HIV-1 and the infected host cells."
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"Taken together, the results show that Nef and USP15 declines were due to expressed protein degradation, and USP15 mediated degradation of Nef was much stronger than Nef mediated USP15 degradation (XREF_FIG)."
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