This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

The understanding of lysosomes has come a long way since the initial discovery of their role
in degrading cellular waste. The lysosome is now recognized as a highly dynamic organelle …

Glial activation and inflammation coincide with neurofibrillary tangle (NFT) formation in
neurons. However, the mechanism behind the interaction between tau fibrils and glia is …

Alzheimer's disease (AD) is defined by intracellular neurofibrillary tangles formed by the
microtubule-associated protein tau and extracellular plaques formed by the β-amyloid …

Pathological tau aggregates cause cognitive decline in neurodegenerative tauopathies,
including Alzheimer's disease (AD). These aggregates are prevalent within intracellular …

The basal forebrain cholinergic neurons (BFCN) provide the primary source of cholinergic
innervation of the human cerebral cortex. They are involved in the cognitive processes of …

Tau is a soluble protein interacting with tubulin to stabilize microtubules. However, under
pathological conditions, it becomes hyperphosphorylated and aggregates, a process that …

Tauopathies are a diverse group of progressive and fatal neurodegenerative diseases
characterized by aberrant tau inclusions in the central nervous system. Tau protein forms …

Tau is a microtubule-associated protein widely distributed in the central nervous system
(CNS). The main function of tau is to promote the assembly of microtubules and stabilize …

The aggregation of misfolded tau into neurotoxic fibrils is linked to the progression of
Alzheimer's disease (AD) and related tauopathies. Disease-associated conformations of …