
IndraLab
Statements
KCNH2 binds NCIT:C17764. 17 / 17
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17
sparser
"To determine the role of chaperone CNX/CRT in the process of ALLN to correct the translocation of HERG-A561V mutant protein, the binding of HERG protein and molecular chaperone CNX/CRT in the HERG-WT, HERG- A561V, HERG-L539fs/47, HERG-WT/A561V, HERG-WT/L539fs/47 cell models were detected by immunoprecipitation after 24-h treatment with or without ALLN (10 μmol/l)."
sparser
"Pharmacological chaperones may serve to disrupt the interaction of immature Kv11.1 proteins with ER chaperone and quality-control proteins including Hsp40 (40-kDa heat shock protein), Hsc70 (70-kDa heat shock cognate protein), Hsp90 (90-kDa heat shock protein), FLBP38, calnexin, and numerous other chaperones, thereby protecting mutant proteins from degradation and alternatively by attenuating digestion by enzymes such as trypsin xref – xref ."
sparser
"This includes the use computational modelling to study the implications of hERG mutations on hERG structure and trafficking, the interactions of hERG with hERG chaperone proteins and with membrane-soluble molecules, the mechanisms of drugs that inhibit hERG trafficking and drugs that rescue hERG mutations."