Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions
Open Access
- 1 July 2005
- journal article
- Published by Elsevier BV
- Vol. 280 (26), 24978-24986
- https://doi.org/10.1074/jbc.m501565200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based TherapeuticsAnnual Review of Pharmacology and Toxicology, 2003
- Toward a Unified Scheme for the Aggregation of Tau into Alzheimer Paired Helical FilamentsBiochemistry, 2002
- Tau story : des démences fronto-temporales aux autres tauopathiesBiologie Aujourd'hui, 2002
- Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical FilamentsBiochemistry, 1999
- A nucleated assembly mechanism of Alzheimer paired helical filamentsProceedings of the National Academy of Sciences of the United States of America, 1998
- Tau in Alzheimer's diseaseTrends in Cell Biology, 1998
- Domains of tau Protein and Interactions with MicrotubulesBiochemistry, 1994
- Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule bindingNeuron, 1993
- Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro.The Journal of cell biology, 1992
- Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.Proceedings of the National Academy of Sciences of the United States of America, 1988