IndraLab

Statements



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"At the molecular level, we find that inhibition of USP14 rapidly triggers accumulation of poly-ubiquitinated proteins and chaperones, mitochondrial dysfunction, ER stress, and a ROS production leading to a caspase independent cell death."

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"Inhibition of USP14 induces ER stress mediated autophagy without apoptosis in lung cancer cell line A549."

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"Notably, in resting cells, USP14 tonically blocks ER associated degradation by interaction with IRE1alpha."

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"USP14 and UCHL5 inhibitors induce accumulation of ubiquitinated proteins and endoplasmic reticulum stress response in ER + BCa."

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"To further investigate whether the ESIs previously reported effect on protein translocation contributed to its inhibitory effect on IL-1 release or whether it was due to an inhibition of DUBs, we investigated the effects of a selective DUB inhibitor b-AP15 and of the protein translocation inhibitor cpd A. b-AP15 is a small molecule DUB inhibitor of the proteasome associated DUBs UCH37 and USP14, whereas cpd A is a selective inhibitor of the ER translocon with no effect on DUB activity."

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"Inhibition of USP14 and UCHL5 activates caspase and triggers apoptosis of ER + BCa cells."

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"Although the physiological role of USP14 mediated inhibition of ERAD must be elucidated, USP14 may serve as a physiological regulator of ERAD to prevent the unnecessary leak of the ER luminal proteins[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"