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- W2066655356 endingPage "532" @default.
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- W2066655356 abstract "Global folding of polypeptides entering the endoplasmic reticulum (ER) starts as soon as they emerge from the narrow Sec61 translocon. Attainment of the native structure can take from several minutes to hours, depending on the gene product. Until then, non-native folding intermediates must be protected from molecular chaperones that recognize misfolded determinants and could prematurely interrupt folding programs by re-directing them to disposal pathways. On the other hand, futile folding attempts must actively be stopped to prevent intraluminal accumulation of defective cargo. This review describes recent advances in understanding how terminally misfolded polypeptides are extracted from the folding environment and directed to specific dislocons within the ER membrane for transfer to the cytoplasm for proteasome-mediated degradation." @default.
- W2066655356 created "2016-06-24" @default.
- W2066655356 creator A5012945125 @default.
- W2066655356 creator A5014309178 @default.
- W2066655356 creator A5040528462 @default.
- W2066655356 date "2010-07-01" @default.
- W2066655356 modified "2023-10-11" @default.
- W2066655356 title "ERAD substrates: Which way out?" @default.
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- W2066655356 doi "https://doi.org/10.1016/j.semcdb.2009.12.007" @default.
- W2066655356 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20026414" @default.
- W2066655356 hasPublicationYear "2010" @default.
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