IndraLab

Statements


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"For instance, the inhibition of the chaperone protein Hsp 90 prevents maturation and promotes the proteasome degradation of hERG protein, thereby reducing the number of mature channels that can be integrated into the cell membrane."

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"7 hERG has been previously identified as an Hsp90 and Hsp70 dependent client protein, and studies have shown that inhibition of Hsp90 with geldanamycin resulted in proteasome mediated degradation of hERG which prevented maturation of a fully functional hERG channel."

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"To assess the involvement of proteasome mediated degradation of hERG proteins, we examined the effects of proteasome inhibitors (lactacystin and ALLN) on the steady state protein levels of WT-hERG, G572R-hERG and E637K-hERG."

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"Most of its mutations give rise to unstable hERG proteins degraded by the proteasome."