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http://purl.uniprot.org/citations/9596579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9596579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9596579http://www.w3.org/2000/01/rdf-schema#comment"MAP kinase phosphatase-3 (MKP-3) dephosphorylates phosphotyrosine and phosphothreonine and inactivates selectively ERK family mitogen-activated protein (MAP) kinases. MKP-3 was activated by direct binding to purified ERK2. Activation was independent of protein kinase activity and required binding of ERK2 to the noncatalytic amino-terminus of MKP-3. Neither the gain-of-function Sevenmaker ERK2 mutant D319N nor c-Jun amino-terminal kinase-stress-activated protein kinase (JNK/SAPK) or p38 MAP kinases bound MKP-3 or caused its catalytic activation. These kinases were also resistant to enzymatic inactivation by MKP-3. Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases. Catalytic activation of MAP kinase phosphatases through substrate binding may regulate MAP kinase activation by a large number of receptor systems."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.org/dc/terms/identifier"doi:10.1126/science.280.5367.1262"xsd:string
http://purl.uniprot.org/citations/9596579http://purl.org/dc/terms/identifier"doi:10.1126/science.280.5367.1262"xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Boschert U."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Boschert U."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Camps M."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Camps M."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Muda M."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Muda M."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Nichols A."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Nichols A."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Antonsson B."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Antonsson B."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Arkinstall S."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Arkinstall S."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Chabert C."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Chabert C."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Gillieron C."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/author"Gillieron C."xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/9596579http://purl.uniprot.org/core/name"Science"xsd:string