Ruggiano, Annamaria, 1985-Foresti, OmbrettaCarvalho, Pedro C.2024-12-092024-12-092014Ruggiano A, Foresti O, Carvalho P. ER-associated degradation: protein quality control and beyond. J Cell Biol. 2014 Mar 17;204(6):869-79. DOI: 10.1083/jcb.2013120420021-9525http://hdl.handle.net/10230/68950Even with the assistance of many cellular factors, a significant fraction of newly synthesized proteins ends up misfolded. Cells evolved protein quality control systems to ensure that these potentially toxic species are detected and eliminated. The best characterized of these pathways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory proteins whose biogenesis takes place in the endoplasmic reticulum (ER). There is also increasing evidence that ERAD controls other ER-related functions through regulated degradation of certain folded ER proteins, further highlighting the role of ERAD in cellular homeostasis.application/pdfeng© 2014 Ruggiano et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).Proteïnes -- AnàlisiVida -- OrigenProteïnes de membranainfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1083/jcb.201312042info:eu-repo/semantics/openAccess