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http://purl.uniprot.org/citations/22665516http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22665516http://www.w3.org/2000/01/rdf-schema#comment"Chaperones and foldases in the endoplasmic reticulum (ER) ensure correct protein folding. Extensive protein-protein interaction maps have defined the organization and function of many cellular complexes, but ER complexes are under-represented. Consequently, chaperone and foldase networks in the ER are largely uncharacterized. Using complementary ER-specific methods, we have mapped interactions between ER-lumenal chaperones and foldases and describe their organization in multiprotein complexes. We identify new functional chaperone modules, including interactions between protein-disulfide isomerases and peptidyl-prolyl cis-trans-isomerases. We have examined in detail a novel ERp72-cyclophilin B complex that enhances the rate of folding of immunoglobulin G. Deletion analysis and NMR reveal a conserved surface of cyclophilin B that interacts with polyacidic stretches of ERp72 and GRp94. Mutagenesis within this highly charged surface region abrogates interactions with its chaperone partners and reveals a new mechanism of ER protein-protein interaction. This ability of cyclophilin B to interact with different partners using the same molecular surface suggests that ER-chaperone/foldase partnerships may switch depending on the needs of different substrates, illustrating the flexibility of multichaperone complexes of the ER folding machinery."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.org/dc/terms/identifier"doi:10.1074/mcp.m111.016550"xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Gehring K."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Thomas D.Y."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Jansen G."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Schade B."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Dejgaard K."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Denisov A.Y."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Maattanen P."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Chen L.Y."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Muller W.J."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Balghi H."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/author"Scarffe L."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/name"Mol Cell Proteomics"xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/pages"710-723"xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/title"An interaction map of endoplasmic reticulum chaperones and foldases."xsd:string
http://purl.uniprot.org/citations/22665516http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/22665516http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22665516
http://purl.uniprot.org/citations/22665516http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22665516
http://purl.uniprot.org/uniprot/P06761#attribution-A9D5C96DC650980A949C13D0E60FBD6Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22665516
http://purl.uniprot.org/uniprot/P18418#attribution-A9D5C96DC650980A949C13D0E60FBD6Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22665516
http://purl.uniprot.org/uniprot/P35565#attribution-A9D5C96DC650980A949C13D0E60FBD6Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22665516
http://purl.uniprot.org/uniprot/Q66HD0#attribution-A9D5C96DC650980A949C13D0E60FBD6Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22665516