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HSP90 activates KCNH2. 8 / 9
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"In the present study, over-expression of Hsp90 increased the mature form of HERG ( Fig. 1 B) but did not affect the level of Kv1.5-FLAG ( Fig. 1 C)."
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"The cytosolic chaperone proteins Hsp70 and Hsp90 were also discovered to bind to hERG and to mediate maturation of hERG subunits."
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"The reduced expression and inhibition of Hsp90 and Hsp70 will significantly decrease the maturation of the hERG protein and accelerate the degradation of the immature protein (Ficker et al., 2003; Li et al., 2011)."
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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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"Hsp90 induced increase of functional HERG proteins was verified by their increased expression on the cell surface and enhanced HERG channel currents."
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"Direct inhibition of Hsp90 by As 2 O 3 is also consistent with the trafficking block of hERG induced by two specific inhibitors of Hsp90 function, geldanamycin and radicicol ( Ficker et al., 2003; Roe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Inhibition of Hsp90 chaperone prevents maturation and increases proteasomal degradation of hERG, reducing the number of mature channels available to be incorporated into the cell membrane."
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"Inhibition of Hsp90 prevents maturation and reduces hERG and IKr currents."
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