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.
MeSH terms
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Alzheimer Disease / pathology*
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Cloning, Molecular
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Escherichia coli
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Humans
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Immunoblotting
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Microscopy, Electron
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Phosphorylation
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / ultrastructure
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tau Proteins / biosynthesis
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tau Proteins / isolation & purification
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tau Proteins / ultrastructure*
Substances
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Recombinant Proteins
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tau Proteins