Pathological aggregation of intrinsically disordered tau protein, driven by the interactions
between microtubule-binding (MTB) domains, is associated with Alzheimer's disease. The …

Tauopathies are a class of neurodegenerative diseases correlated with the presence of
pathological Tau fibrils as a diagnostic marker. The microtubule-binding repeat region of …

Hypochlorous acid (HOCl) released from activated leukocytes not only plays a significant
role in the human immune system but is also implicated in numerous diseases including …

The accumulation of ΔK280 tau mutant resulting in neurotoxic oligomeric aggregates is an
important but yet mysterious procedure in Alzheimer's disease (AD) development. Recently …

Tau misfolding plays a significant role in some neurodegenerative diseases such as
Alzheimer's disease (AD). It is intrinsically disordered and highly soluble under normal …

The aggregation and structural conversion of normal prion peptide (PrPC) into the
pathogenic scrapie form (PrPSc), which can act as a seed to enhance prion amyloid fiber …

Early oligomerization of human islet amyloid polypeptide (hIAPP), which is accountable for β‐
cell death, has been implicated in the progression of type 2 diabetes mellitus. Some …

Research on misfolding of tau proteins will help to better understand the formation process
of neurofibrillary tangles, a hallmark of Alzheimer's disease. Mutation and histidine …

Monitoring early-stage β-amyloid (Aβ) dimerization is a formidable challenge for
understanding neurological diseases. We compared β-sheet formation and histidine site …

Controlling protein misfolding and accumulation in neurodegeneration is a challenge in
chemical neuroscience. The application of appropriate electric fields (EFs) can be a …