IndraLab
Statements
KCNH2 binds NCIT:C17764. 18 / 18
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18
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."
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 ."