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http://purl.uniprot.org/citations/15848158http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15848158http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15848158http://www.w3.org/2000/01/rdf-schema#comment"Both amyloid-prone cystatin and unstable mutant C94A lysozyme were secreted in wild-type and Deltaeps1 Saccharomyces cerevisiae cells. Amyloid-prone cystatin secreted at much higher level in Deltaeps1 cells than that in wild-type yeast. In parallel, the secretion amount of disulfide bond disrupted mutant C94A lysozyme greatly increased in Deltaeps1 cells although that was apparently low in wild-type yeast cells compared with the secretion amount of wild-type lysozyme. It is interesting that neither the unstable mutant C94A lysozyme nor amyloid-prone cystatin secreted in Deltaeps1 cells maintained their specific activities. These observations lead to the supposition that yeast cells deficient for the protein disulfide isomerase-family-member EPS1 locus secrete more of labile disulfide-containing model proteins."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2005.03.019"xsd:string
http://purl.uniprot.org/citations/15848158http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2005.03.019"xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"He J."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"He J."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Kato A."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Kato A."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Song Y."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Song Y."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Saito A."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Saito A."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Azakami H."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Azakami H."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Harada A."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Harada A."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Sakamoto T."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/author"Sakamoto T."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/pages"2277-2283"xsd:string
http://purl.uniprot.org/citations/15848158http://purl.uniprot.org/core/pages"2277-2283"xsd:string