1. Assembly of Alzheimer-like filaments from full-length tau protein
- Author
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R.A. Crowther, Michel Goedert, O.F. Olesen, Ross Jakes, and Michael J. Smith
- Subjects
Hyper-phosphorylation ,Microtubule-associated protein tau ,Immunoblotting ,Tau protein ,Biophysics ,tau Proteins ,macromolecular substances ,Biology ,Biochemistry ,law.invention ,Protein filament ,Degenerative disease ,Alzheimer Disease ,Structural Biology ,Microtubule ,law ,Escherichia coli ,Genetics ,medicine ,Humans ,Cloning, Molecular ,Phosphorylation ,Molecular Biology ,Cell Biology ,Anatomy ,Alzheimer's disease ,medicine.disease ,Recombinant Proteins ,In vitro ,Paired helical filament ,Microscopy, Electron ,Recombinant DNA ,biology.protein - Abstract
The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease.
- Published
- 1994
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