The polymerization of the microtubule-associated protein, tau, into insoluble filaments is common to Alzheimer's disease (AD) and in a variety of dementias. The conformational change required for tau to transition from soluble monomers to filamentous AD pathology involves the extreme N-terminus of tau coming into contact with other regions of...
Neurofibrillary tangle (NFT) formation in Alzheimer's disease (AD) and tauopathies occurs when tau protein adopts secondary structure and self-aggregates within neurons. Accompanying NFT maturation are post-translational modifications to tau; hyperphosphorylation, truncation and conformational changes occur in a highly sequential manner. In contrast, granulovacuolar degeneration bodies (GVDs) are a second type...
In several neurodegenerative diseases, the microtubule-associated protein tau self-aggregates to form filaments that accumulate in neurons and/or glia, although the relationship between tau aggregation and cell death is a subject of debate. The amino terminus of tau is involved in conformational changes that appear critical for filament formation, hinting at...