Phosphorylation by Neuronal cdc2-like Protein Kinase Promotes Dimerization of Tau Protein in Vitro
Open Access
- 1 November 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (45) , 28328-28334
- https://doi.org/10.1074/jbc.272.45.28328
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycansNature, 1996
- Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments.Proceedings of the National Academy of Sciences, 1995
- Dephosphorylation of Alzheimer Paired Helical Filaments by Protein Phosphatase-2A and −2BJournal of Biological Chemistry, 1995
- Proline-directed and Non-proline-directed Phosphorylation of PHF-tauJournal of Biological Chemistry, 1995
- Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.Proceedings of the National Academy of Sciences, 1994
- Tau protein and the neurofibrillary pathology of Alzheimer's diseaseTrends in Neurosciences, 1993
- The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's diseaseFEBS Letters, 1992
- Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro.The Journal of cell biology, 1992
- A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal TauScience, 1991
- Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's diseaseNeuron, 1989