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http://purl.uniprot.org/citations/15208260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15208260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15208260http://www.w3.org/2000/01/rdf-schema#comment"Potentially toxic amyloid beta-peptide (Abeta) in Alzheimer's disease (AD) is generated from a family of Abeta-containing precursor proteins (APP), which is regulated via the 5'-untranslated region (5'-UTR) of its mRNA. We analyzed 5'-UTRs of the APP superfamily, including amyloid plaque-forming and non-amyloid plaque-forming species, and of prions (27 different DNA sequences). A "CAGA" sequence proximal to the "ATG" start codon was present in a location unique to APP genes of amyloid plaque-forming species and absent in all other genes surveyed. This CAGA box is immediately upstream of an interleukin-1-responsive element (acute box). In addition, the proximal CAGA box is predicted to appear on a stem-loop structure in both human and guinea pig APP mRNA. This stem-loop is part of a predicted bulge-loop that encompasses a known iron regulatory element (IRE). Electrophoretic mobility shift with segments of the APP 5'-UTR showed that a region with the proximal CAGA sequence binds nuclear proteins, and this UTR fragment is active in a reporter gene functional assay. Thus, the 5'-UTR in the human APP but not those of APP-like proteins contains a specific region that may participate in APP regulation and may determine a more general model for amyloid generation as seen in AD. The 5'-UTR of human APP contains several interesting control elements, such as an acute box element, a CAGA box, an IRE, and a transforming growth factor-beta-responsive element, that could control APP expression and provide suitable and specific drug targets for AD."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.org/dc/terms/identifier"doi:10.1096/fj.03-1703fje"xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Lahiri D.K."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Lahiri D.K."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Ge Y.W."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Ge Y.W."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Greig N."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Greig N."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Maloney B."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/author"Maloney B."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/name"FASEB J."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/name"FASEB J"xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/pages"1288-1290"xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/pages"1288-1290"xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/title"Presence of a 'CAGA box' in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/title"Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/15208260http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/15208260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15208260
http://purl.uniprot.org/citations/15208260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15208260
http://purl.uniprot.org/citations/15208260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15208260