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http://purl.uniprot.org/citations/10319819http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10319819http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10319819http://www.w3.org/2000/01/rdf-schema#comment"The amyloid-beta precursor protein (APP) is directly and efficiently cleaved by caspases during apoptosis, resulting in elevated amyloid-beta (A beta) peptide formation. The predominant site of caspase-mediated proteolysis is within the cytoplasmic tail of APP, and cleavage at this site occurs in hippocampal neurons in vivo following acute excitotoxic or ischemic brain injury. Caspase-3 is the predominant caspase involved in APP cleavage, consistent with its marked elevation in dying neurons of Alzheimer's disease brains and colocalization of its APP cleavage product with A beta in senile plaques. Caspases thus appear to play a dual role in proteolytic processing of APP and the resulting propensity for A beta peptide formation, as well as in the ultimate apoptotic death of neurons in Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)80748-5"xsd:string
http://purl.uniprot.org/citations/10319819http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)80748-5"xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Xu D."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Xu D."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Smith D."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Smith D."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Zhu Y."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Zhu Y."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Zheng H."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Zheng H."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Roy S."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Roy S."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"van der Ploeg L.H.T."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"van der Ploeg L.H.T."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Clarke E.E."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Clarke E.E."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Gervais F.G."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"Gervais F.G."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"LeBlanc A."xsd:string
http://purl.uniprot.org/citations/10319819http://purl.uniprot.org/core/author"LeBlanc A."xsd:string