IndraLab

Statements


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"However, when expressed alone, USP15 inhibited the IFN signaling pathway."

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"These results together suggested that both USP15 constructed in two different expression plasmids inhibited the production of IFN."

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"Although we can not rule out the possibility that USP15 exerts its effects in a third uncharacterized manner, the data in this study demonstrate that USP15 sequesters the interaction between RIG-I and IPS-1, shedding light on the mechanisms underlying the catalytic-activity-independent antagonism of IFN by USP15."

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"To verify the specific mechanism of USP15 mediated IFN inhibition, we identified the DUB activity site His862 of USP15 in vivo and in vitro, and we presented evidence that USP15 functions as a RIG-I deubiquitinase and specifically removes Lys63 linked polyubiquitin chains."

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"Taken together, we showed that in contrast to miR-26a, USP15 negatively regulated the type I IFN response to facilitate virus replication."

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"USP15 negatively regulates type I IFN signaling to promote virus replication."

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"Furthermore , USP15 can be recruited by ubiquitin-conjugating enzyme UBE2S ( E2 ) to deubiquitylates TBK1 , inhibiting type I IFN production ( Huang et al ., 2020 ) ."

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"In a study using HEK293T cells and Sendai virus (SeV), knockdown of the gene transcribing USP15 resulted in upregulation of type I IFN, while overexpression of USP15 decreased type I interferon as USP15 showed dose dependent inhibition of IFN-beta [XREF_BIBR]."

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"Reminding us USP15 may antagonize type I IFN induction independently of catalytic activity."