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...
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...
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...