IndraLab

Statements

ICP0 inhibits USP7. 7 / 7
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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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"ICP0 also disrupts NF-kappaB activation by subverting the activity of the cellular deubiquitylating enzyme USP7."
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"Recent studies reported reciprocal activities between both enzymes with a dominant effect of USP7-mediated stabilization of ICP0 over ICP0-induced degradation of USP7 during productive HSV-1 infection[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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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"ICP0 Directs the Degradation of USP7, a Mediator of Intrinsic and Innate Immunity."
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"Conversely ICP0 induces the degradation of USP7 [XREF_BIBR]."
26046769
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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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