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http://purl.uniprot.org/citations/22119785http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22119785http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22119785http://www.w3.org/2000/01/rdf-schema#comment"Proteins that fail to correctly fold or assemble into oligomeric complexes in the endoplasmic reticulum (ER) are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). Although many individual components of the ERAD system have been identified, how these proteins are organized into a functional network that coordinates recognition, ubiquitylation and dislocation of substrates across the ER membrane is not well understood. We have investigated the functional organization of the mammalian ERAD system using a systems-level strategy that integrates proteomics, functional genomics and the transcriptional response to ER stress. This analysis supports an adaptive organization for the mammalian ERAD machinery and reveals a number of metazoan-specific genes not previously linked to ERAD."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.org/dc/terms/identifier"doi:10.1038/ncb2383"xsd:string
http://purl.uniprot.org/citations/22119785http://purl.org/dc/terms/identifier"doi:10.1038/ncb2383"xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Sowa M.E."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Sowa M.E."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Harper J.W."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Harper J.W."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Kopito R.R."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Kopito R.R."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Olzmann J.A."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Olzmann J.A."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Tyler R.E."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Tyler R.E."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Bennett E.J."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Bennett E.J."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Christianson J.C."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Christianson J.C."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Shaler T.A."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Shaler T.A."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Greenblatt E.J."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Greenblatt E.J."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Richter C.M."xsd:string
http://purl.uniprot.org/citations/22119785http://purl.uniprot.org/core/author"Richter C.M."xsd:string