Regulation of the Phosphorylation State and Microtubule-Binding Activity of Tau by Protein Phosphatase 2A
- 1 December 1996
- Vol. 17 (6) , 1201-1207
- https://doi.org/10.1016/s0896-6273(00)80250-0
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcmeurin and phosphatase‐2APublished by Wiley ,2001
- In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neuronsFEBS Letters, 1995
- Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205Neuroscience Letters, 1995
- Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer diseaseFEBS Letters, 1994
- The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferationCell, 1993
- Tau protein and the neurofibrillary pathology of Alzheimer's diseaseTrends in Neurosciences, 1993
- Abnormal tau phosphorylation at Ser396 in alzheimer's disease recapitulates development and contributes to reduced microtubule bindingNeuron, 1993
- p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's diseaseFEBS Letters, 1992
- Immunological and conformational characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's diseaseBiochemical and Biophysical Research Communications, 1992
- A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal TauScience, 1991