RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11146006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11146006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11146006http://www.w3.org/2000/01/rdf-schema#comment"Threonine(668) (thr(668)) within the carboxy-terminus of the Alzheimer's disease amyloid precursor protein (APP) is a known in vivo phosphorylation site. Phosphorylation of APPthr(668) is believed to regulate APP function and metabolism. Thr(668) precedes a proline, which suggests that it is targeted for phosphorylation by proline-directed kinase(s). We have investigated the ability of four major neuronally active proline-directed kinases, cyclin dependent protein kinase-5, glycogen synthase kinase-3 beta, p42 mitogen-activated protein kinase and stress-activated protein kinase-1b, to phosphorylate APPthr(668) and report here that SAPK1b induces robust phosphorylation of this site both in vitro and in vivo. This finding provides a molecular framework to link cellular stresses with APP metabolism in both normal and disease states."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.org/dc/terms/identifier"doi:10.1046/j.1471-4159.2001.00102.x"xsd:string
http://purl.uniprot.org/citations/11146006http://purl.org/dc/terms/identifier"doi:10.1046/j.1471-4159.2001.00102.x"xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Brownlees J."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Brownlees J."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Grierson A.J."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Grierson A.J."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Kesavapany S."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Kesavapany S."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Lau K.-F."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Lau K.-F."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"McLoughlin D.M."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"McLoughlin D.M."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Miller C.C.J."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Miller C.C.J."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Standen C.L."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/author"Standen C.L."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/pages"316-320"xsd:string
http://purl.uniprot.org/citations/11146006http://purl.uniprot.org/core/pages"316-320"xsd:string