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pubmed-article:12612637pubmed:dateCreated2003-3-3lld:pubmed
pubmed-article:12612637pubmed:abstractTextThe endoplasmic reticulum (ER) has a quality-control system for 'proof-reading' newly synthesized proteins, so that only native conformers reach their final destinations. Non-native conformers and incompletely assembled oligomers are retained, and, if misfolded persistently, they are degraded. As a large fraction of ER-synthesized proteins fail to fold and mature properly, ER quality control is important for the fidelity of cellular functions. Here, we discuss recent progress in understanding the conformation-specific sorting of proteins at the level of ER retention and export.lld:pubmed
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pubmed-article:12612637pubmed:authorpubmed-author:HeleniusAriAlld:pubmed
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pubmed-article:12612637pubmed:year2003lld:pubmed
pubmed-article:12612637pubmed:articleTitleQuality control in the endoplasmic reticulum.lld:pubmed
pubmed-article:12612637pubmed:affiliationInstitute of Biochemistry, Swiss Federal Institute of Technology (ETH) Zürich, Hönggerberg, CH - 8093 Zürich, Switzerland.lld:pubmed
pubmed-article:12612637pubmed:publicationTypeJournal Articlelld:pubmed
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pubmed-article:12612637pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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