Phosphorylation of Microtubule-associated Protein Tau Is Regulated by Protein Phosphatase 2A in Mammalian Brain
Open Access
- 1 February 2000
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 275 (8), 5535-5544
- https://doi.org/10.1074/jbc.275.8.5535
Abstract
No abstract availableKeywords
This publication has 73 references indexed in Scilit:
- Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tauProceedings of the National Academy of Sciences, 1997
- Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubulesNature Medicine, 1996
- Restoration of biological activity of Alzheimer abnormally phosphorylated τ by dephosphorylation with protein phosphatase-2A, −2B and −1Molecular Brain Research, 1996
- Dephosphorylation of Alzheimer Paired Helical Filaments by Protein Phosphatase-2A and −2BJournal of Biological Chemistry, 1995
- Alzheimer paired helical filaments Restoration of the biological activity by dephosphorylationFEBS Letters, 1994
- Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.Proceedings of the National Academy of Sciences, 1994
- A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal TauScience, 1991
- Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease.Proceedings of the National Academy of Sciences, 1989
- Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's diseaseBrain Research, 1989
- Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.Proceedings of the National Academy of Sciences, 1986