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http://purl.uniprot.org/citations/20364150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20364150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20364150http://www.w3.org/2000/01/rdf-schema#comment"Most antigenic peptides presented by major histocompatibility complex (MHC) class I molecules are produced by the proteasome. Here we show that a proteasome-independent peptide derived from the human tumor protein MAGE-A3 is produced directly by insulin-degrading enzyme (IDE), a cytosolic metallopeptidase. Cytotoxic T lymphocyte recognition of tumor cells was reduced after metallopeptidase inhibition or IDE silencing. Separate inhibition of the metallopeptidase and the proteasome impaired degradation of MAGE-A3 proteins, and simultaneous inhibition of both further stabilized MAGE-A3 proteins. These results suggest that MAGE-A3 proteins are degraded along two parallel pathways that involve either the proteasome or IDE and produce different sets of antigenic peptides presented by MHC class I molecules."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.org/dc/terms/identifier"doi:10.1038/ni.1862"xsd:string
http://purl.uniprot.org/citations/20364150http://purl.org/dc/terms/identifier"doi:10.1038/ni.1862"xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Stroobant V."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Stroobant V."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Morel S."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Morel S."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Van den Eynde B.J."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Van den Eynde B.J."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Parmentier N."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Parmentier N."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Chapiro J."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Chapiro J."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Colau D."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"Colau D."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"de Diesbach P."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"de Diesbach P."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"van Endert P."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/author"van Endert P."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/name"Nat. Immunol."xsd:string
http://purl.uniprot.org/citations/20364150http://purl.uniprot.org/core/name"Nat. Immunol."xsd:string