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dc.contributor.authorHebert, Daniel N
dc.contributor.authorMolinari, Maurizio
dc.date2022-08-11T08:08:57.000
dc.date.accessioned2022-08-23T16:13:50Z
dc.date.available2022-08-23T16:13:50Z
dc.date.issued2007-10-12
dc.date.submitted2008-09-11
dc.identifier.citationPhysiol Rev. 2007 Oct;87(4):1377-408. <a href="http://dx.doi.org/10.1152/physrev.00050.2006">Link to article on publisher's site</a>
dc.identifier.issn0031-9333 (Print)
dc.identifier.doi10.1152/physrev.00050.2006
dc.identifier.pmid17928587
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33718
dc.description.abstractA substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter cotranslationally in the ER lumen, which contains resident molecular chaperones and folding factors that assist their maturation. Native proteins are released from the ER lumen and are transported through the secretory pathway to their final intra- or extracellular destination. Folding-defective polypeptides are exported across the ER membrane into the cytosol and destroyed. Cellular and organismal homeostasis relies on a balanced activity of the ER folding, quality control, and degradation machineries as shown by the dozens of human diseases related to defective maturation or disposal of individual polypeptides generated in the ER.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=17928587&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1152/physrev.00050.2006
dc.subjectEndoplasmic Reticulum; Humans; Metabolic Diseases; Molecular Chaperones; Protein Biosynthesis; *Protein Folding
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleIn and out of the ER: protein folding, quality control, degradation, and related human diseases
dc.typeJournal Article
dc.source.journaltitlePhysiological reviews
dc.source.volume87
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/380
dc.identifier.contextkey626931
html.description.abstract<p>A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter cotranslationally in the ER lumen, which contains resident molecular chaperones and folding factors that assist their maturation. Native proteins are released from the ER lumen and are transported through the secretory pathway to their final intra- or extracellular destination. Folding-defective polypeptides are exported across the ER membrane into the cytosol and destroyed. Cellular and organismal homeostasis relies on a balanced activity of the ER folding, quality control, and degradation machineries as shown by the dozens of human diseases related to defective maturation or disposal of individual polypeptides generated in the ER.</p>
dc.identifier.submissionpathgsbs_sp/380
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages1377-408


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