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ICP0 inhibits USP7. 8 / 8
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"For example, ICP0 was reported to interact with and degrade USP7, which is a deubiquitylating enzyme like USP9X, but one that promotes HSV-1 replication by reversing ICP0 self ubiquitination [XREF_BIBR, XREF_BIBR]."

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"Taken together, these data indicate that ICP0 can interact with and promote the proteasome dependent degradation of both USP7 and USP7 beta during HSV-1 infection.ICP0 belongs to the RING-finger class[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"ICP0 also disrupts NF-kappaB activation by subverting the activity of the cellular deubiquitylating enzyme USP7."

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"It is noteworthy that the synthesis of both negative- and plus-strand coronavirus RNA requires ongoing viral protein production (Kim et al., 1995, Perlman et al., 1986, Sawicki and Sawicki, 1986), and it is conceivable that concomitant deubiquitination by SARS-CoV PLpro protects replicase subunits against proteasomal degradation.Prompted by the known interaction of ICP0 with cellular USP7, Ploegh and coworkers made use of the active-site directed probe HAUbVME, mentioned above, to monitor DUB activity in lysates of primary fibroblasts infected with HSV-1 (Kattenhorn et al., 2005)."

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"Conversely ICP0 induces the degradation of USP7 [XREF_BIBR]."

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"The fundamental conclusion of these studies is that depletion of USP7 destabilized ICP0, that ICP0 mediated the degradation of USP7, and that amino acid substitutions in ICP0 that abolished binding to USP7 significantly impaired the ability of HSV-1 to replicate."

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"It is noteworthy that the synthesis of both negative-and plus-strand coronavirus RNA requires ongoing viral protein production (Kim et al., 1995; Perlman et al., 1986; Sawicki and Sawicki, 1986) , and it is conceivable that concomitant deubiquitination by SARS-CoV PLpro protects replicase subunits against proteasomal degradation.Prompted by the known interaction of ICP0 with cellular USP7, Ploegh and coworkers made use of the active-site directed probe HAUbVME, mentioned above, to monitor DUB activity in lysates of primary fibroblasts infected with HSV-1 ."

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"ICP0 Directs the Degradation of USP7, a Mediator of Intrinsic and Innate Immunity."