FEBS Letters · 1992 · 507 citations · 29 references
Life SciencesMolecular BiologyNeuroscienceMolecular NeuroscienceNeurodegenerationSignal TransductionAlzheimer DiseaseAmyloid FormationMicrotubule-associated ProteinsNeurodegenerative DiseasesNeurodegenerative DisordersTau PathologyAlzheimer Disease Tau PathologyGlycogen Synthase Kinase 3 RegulationGlycogen Synthase Kinase 3 SignalingGlycogen Synthase Kinase RegulationPaired Helical FilamentsPeptide EpitopesTau AggregationTau Protein Aggregation
The Alzheimer-like state of tau protein includes phosphorylation by a proline-directed Ser/Thr kinase present in normal or pathological human brain. Extending earlier results on MAP kinase, we show here that the proline-directed kinase, GSK3, can induce an Alzheimer-like immune response involving several distinct and phosphorylatable epitopes at Ser-Pro motifs, as well as a gel mobility shift, similar to MAP kinase. Both kinases behave like microtubule-associated proteins in that they co-purify through cycles of assembly and disassembly, and both kinases are directly associated with paired helical filaments.
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A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
Virginia M.‐Y. Lee, Brian J. Balin, László Ötvös et al. · Science · 1991 · 1.4K citations