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Fibrils composed of tau protein are a pathological hallmark of several neurodegenerative disorders including Alzheimer's disease (AD). Here we show that when recombinant tau protein is seeded with paired helical filaments (PHFs) isolated from AD brain, the amyloid formed shares many of the structural features of AD PHFs. In contrast, tau amyloids formed(More)
Tauopathies encompass a broad family of neurodegenerative diseases, including Alzheimer's disease, which are characterized by the fibrillization of the microtubule-associated tau protein. The normal function of tau is to stabilize and promote the assembly of microtubules in neuronal axons. Sequestration of tau into amyloid fibrils results in destabilization(More)
Many neurodegenerative diseases are associated with deposits of aggregated protein in the brain. The molecular pathways through which soluble proteins misfold to form amyloids and large protein aggregates often include diverse oligomeric species, only some of which progress to the amyloid state. Here we show that prefibrillar huntingtin (HTT) oligomers,(More)
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