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• W2130188329 endingPage "820" @default.
• W2130188329 startingPage "815" @default.
• W2130188329 abstract "Proteins entering the endoplasmic reticulum (ER) have to acquire an export-competent structure before they are delivered to their final destination. This folding process is monitored by an ER protein quality control system. Folding-incompetent conformers are eliminated via a mechanism called ER-associated protein degradation (ERAD). Genetic studies in the yeast Saccharomyces cerevisiae have revealed that carbohydrate modification plays a crucial role in these processes. Here we show that a previously isolated der mutant (der7-1) is defective in ERAD. We identify DER7 as the gene encoding N-glycan-processing α-glucosidase I (EC 3.2.1.106) of the ER and demonstrate that its inactivity, due to a substitution of the conserved glycine residue at position 725 by arginine (G725R) in the der7-1 mutant, leads to ER-stress." @default.
• W2130188329 created "2016-06-24" @default.
• W2130188329 creator A5017405954 @default.
• W2130188329 creator A5084814331 @default.
• W2130188329 date "2004-09-01" @default.
• W2130188329 modified "2023-09-27" @default.
• W2130188329 title "DER7, encoding α-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum" @default.
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• W2130188329 doi "https://doi.org/10.1016/j.femsyr.2004.04.002" @default.
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