IndraLab

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"Our studies indicate that apoptosis can be modulated by peroxisomal import of USP2, resulting in its spatial separation from its target proteins in the cytosol and nucleus."

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"Caspase dependent apoptosis caused by overexpression of USP2 was first described for USP2-2 [XREF_BIBR] but also for isoform 1 [XREF_BIBR]."

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"Hence, the USP2 variants seem to cause the activation of apoptosis pathways by the specific stabilising of their RIP1 substrate.Based on the pro apoptotic effect when USP2c was targeted by RNAi, we fo[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In vitro an artificial knockdown of USP2 inhibited actinomycin D/TNFalpha induced hepatocyte apoptosis, which was associated with elevated levels of the anti-apoptotic protein c-Flip (L/S) and a concomitant decrease of cellular levels of the ubiquitinligase Itch, a negative regulator of c-Flip."

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"Significantly , siRNA knockdown of USP2 resulted in apoptosis , which could be reversed by overexpression of fatty acid synthase ( FAS ) ( 8) ."

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"We have previously shown that the 41 kDa USP2 isoform induces apoptosis [3] and that the 69 kDa USP2a isoform mediates the apoptosis signal of the TNF receptor [5]."

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"Knockdown of USP2 did not increase cell apoptosis in Hut-78 cells compared to cells with control siRNA, further suggesting the pivotal role of p53 in USP2 function."