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http://purl.uniprot.org/citations/11544248http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11544248http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11544248http://www.w3.org/2000/01/rdf-schema#comment"The beta-amyloid precursor protein (APP) is a ubiquitous receptor-like molecule without a known function. However, the recent recognition that APP and Notch undergo highly similar proteolytic processing has suggested a potential signaling function for APP. After ligand binding, Notch is cleaved by the ADAM-17 metalloprotease followed by an intramembrane cleavage mediated by gamma-secretase. The gamma-secretase cut releases the Notch intracellular domain (NICD), which enters the nucleus and modulates transcription. Because APP is processed similarly by ADAM-17 and gamma-secretase, we reasoned that the APP intracellular domain (AICD) has a role analogous to the NICD. We therefore generated a plasmid encoding the AICD sequence and studied the subcellular localization of the expressed protein (C60). Our results demonstrate that the cytoplasmic domain of APP is a highly labile fragment that is stabilized by forming complexes with Fe65 and can then enter the nucleus in neurons and non-neural cells. These findings strongly support the hypothesis that APP signals in the nucleus in a manner analogous to the function of Notch."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100447200"xsd:string
http://purl.uniprot.org/citations/11544248http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100447200"xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Guenette S.Y."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Guenette S.Y."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Selkoe D.J."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Selkoe D.J."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Kimberly W.T."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Kimberly W.T."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Zheng J.B."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/author"Zheng J.B."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/pages"40288-40292"xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/pages"40288-40292"xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/title"The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/title"The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner."xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11544248http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11544248http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11544248
http://purl.uniprot.org/citations/11544248http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11544248