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http://purl.uniprot.org/citations/11943212http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11943212http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11943212http://www.w3.org/2000/01/rdf-schema#comment"Tau is a microtubule-associated protein that is abnormally hyperphosphorylated in the filamentous lesions that define a number of neurodegenerative diseases collectively referred to as tauopathies. We previously showed that stress-activated protein (SAP) kinases phosphorylate tau protein at many of the hyperphosphorylated sites in vitro. Here we have developed a system to study the effects of five SAP kinases (SAPK1c/JNK1, SAPK2a/p38alpha, SAPK2b/p38beta, SAPK3/p38gamma and SAPK4/p38delta) on tau phosphorylation in intact cells. All kinases phosphorylated tau, albeit at different efficiencies. Tau was a good substrate for SAPK3/p38gamma and SAPK4/p38delta, a reasonable substrate for SAPK2b/p38beta and a relatively poor substrate for SAPK2a/p38alpha and SAPK1c/JNK1. These findings indicate that the aberrant activation of SAP kinases, especially SAPK3/p38gamma and SAPK4/p38delta, could play an important role in the abnormal hyperphosphorylation of tau that is an invariant feature of the tauopathies."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(02)02460-2"xsd:string
http://purl.uniprot.org/citations/11943212http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(02)02460-2"xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/author"Goedert M."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/author"Goedert M."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/author"Buee-Scherrer V."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/author"Buee-Scherrer V."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/pages"151-154"xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/pages"151-154"xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/title"Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/title"Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells."xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/volume"515"xsd:string
http://purl.uniprot.org/citations/11943212http://purl.uniprot.org/core/volume"515"xsd:string
http://purl.uniprot.org/citations/11943212http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11943212
http://purl.uniprot.org/citations/11943212http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11943212
http://purl.uniprot.org/citations/11943212http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11943212
http://purl.uniprot.org/citations/11943212http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11943212
http://purl.uniprot.org/uniprot/O15264http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11943212
http://purl.uniprot.org/uniprot/O15264#attribution-F3A16FF454BD81E91383A243952E97A6http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/11943212