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http://purl.uniprot.org/citations/28257000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28257000http://www.w3.org/2000/01/rdf-schema#comment"Unfavorable redox conditions in the endoplasmic reticulum (ER) can decrease the capacity for protein secretion, altering vital cell functions. While systems to manage reductive stress are well-established, how cells cope with an overly oxidizing ER remains largely undefined. In previous work (Wang et al., 2014), we demonstrated that the chaperone BiP is a sensor of overly oxidizing ER conditions. We showed that modification of a conserved BiP cysteine during stress beneficially alters BiP chaperone activity to cope with suboptimal folding conditions. How this cysteine is reduced to reestablish 'normal' BiP activity post-oxidative stress has remained unknown. Here we demonstrate that BiP's nucleotide exchange factor - Sil1 - can reverse BiP cysteine oxidation. This previously unexpected reductant capacity for yeast Sil1 has potential implications for the human ataxia Marinesco-Sjögren syndrome, where it is interesting to speculate that a disruption in ER redox-signaling (due to genetic defects in SIL1) may influence disease pathology."xsd:string
http://purl.uniprot.org/citations/28257000http://purl.org/dc/terms/identifier"doi:10.7554/elife.24141"xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/author"Sevier C.S."xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/author"Pareja K.A."xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/author"Siegenthaler K.D."xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/pages"e24141"xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/title"An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP."xsd:string
http://purl.uniprot.org/citations/28257000http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/28257000http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28257000
http://purl.uniprot.org/citations/28257000http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28257000
http://purl.uniprot.org/uniprot/#_A0A8H4BUM1-mappedCitation-28257000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/#_A0A8H4BYJ9-mappedCitation-28257000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/#_P16474-mappedCitation-28257000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/#_Q08199-mappedCitation-28257000http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/A0A8H4BUM1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/Q08199http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/A0A8H4BYJ9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28257000
http://purl.uniprot.org/uniprot/P16474http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28257000