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"The inhibition of NF-κB activation by USP31 was not due to a reduction of effector protein expression, since Western blot analysis revealed that the levels of all effector proteins were unaffected by [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Here, we show that maybe the stability of NF-kappaB is controlled by proteasome mediated degradation and ubiquitin specific protease 48 (USP48), also known as synaptic ubiquitin specific protease (synUSP) or USP31, can enhance NF-kappaB stability through proteasome dependent regulation in the nucleus."

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"However, subsequent studies demonstrated that in fact USP48 promotes NF-kappaB activity by co-operating with the COP9 signalosome to trim K48 linked polyubiquitin chains from p65 in the nucleus [XREF_BIBR]."