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- W2034289224 endingPage "539" @default.
- W2034289224 startingPage "533" @default.
- W2034289224 abstract "During protein synthesis, the orderly progression of folding, modification, and assembly is paramount to function and vis-à-vis cellular viability. Accordingly, sophisticated quality control mechanisms have evolved to monitor protein maturation throughout the cell. Proteins failing at any step are segregated and degraded as a preventative measure against potential toxicity. Although protein quality control is generally poorly understood, recent research advances in endoplasmic reticulum-associated degradation (ERAD) pathways have provided the most detailed view so far. The discovery of distinct substrate processing sites established a biochemical basis for genetic profiles of model misfolded proteins. Detailed mechanisms for substrate recognition were recently uncovered. For some proteins, sequential glycan trimming steps set a time window for folding. Proteins still unfolded at the final stage expose a specific degradation signal recognized by the ERAD machinery. Through this mechanism, the system does not in fact know that a molecule is misfolded. Instead, it goes by the premise that proteins past due have veered off their normal folding pathways and therefore aberrant." @default.
- W2034289224 created "2016-06-24" @default.
- W2034289224 creator A5037760343 @default.
- W2034289224 creator A5081732668 @default.
- W2034289224 date "2010-07-01" @default.
- W2034289224 modified "2023-10-18" @default.
- W2034289224 title "ERAD substrate recognition in budding yeast" @default.
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