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http://purl.uniprot.org/citations/14517339http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14517339http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14517339http://www.w3.org/2000/01/rdf-schema#comment"Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are a functionally and structurally diverse family of post-translationally modified membrane proteins found mostly in the outer leaflet of the plasma membrane in a variety of eukaryotic cells. Although the general role of GPI-APs remains unclear, they have attracted attention because they act as enzymes and receptors in cell adhesion, differentiation, and host-pathogen interactions. GPI-APs may represent potential diagnostic and therapeutic targets in humans and are interesting in plant biotechnology because of their key role in root development. We here present a general mass spectrometry-based proteomic "shave-and-conquer" strategy that specifically targets GPI-APs. Using a combination of biochemical methods, mass spectrometry, and computational sequence analysis we identified six GPI-APs in a Homo sapiens lipid raft-enriched fraction and 44 GPI-APs in an Arabidopsis thaliana membrane preparation, representing the largest experimental dataset of GPI-anchored proteins to date."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.org/dc/terms/identifier"doi:10.1074/mcp.m300079-mcp200"xsd:string
http://purl.uniprot.org/citations/14517339http://purl.org/dc/terms/identifier"doi:10.1074/mcp.m300079-mcp200"xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Foster L.J."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Foster L.J."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Jensen O.N."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Jensen O.N."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Nuehse T.S."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Nuehse T.S."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Peck S.C."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Peck S.C."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Stensballe A."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Stensballe A."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Elortza F."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/author"Elortza F."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/name"Mol. Cell. Proteomics"xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/name"Mol. Cell. Proteomics"xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/pages"1261-1270"xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/pages"1261-1270"xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/title"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."xsd:string
http://purl.uniprot.org/citations/14517339http://purl.uniprot.org/core/title"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."xsd:string