Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Alzheimer's disease (AD) is pathologically defined by extracellular accumulation of amyloid-
β (Aβ) peptides generated by the cleavage of amyloid precursor protein (APP), strings of …

Protein misfolding is a general hallmark of protein deposition diseases, such as Alzheimer's
disease or Parkinson's disease, in which different types of aggregated species (oligomers …

The progressive accumulation of insoluble aggregates of the presynaptic protein alpha-
synuclein (α-Syn) is a hallmark of neurodegenerative disorders including Parkinson's …

Abnormal accumulation of misfolded tau aggregates is a pathological hallmark of various
tauopathies including Alzheimer's disease (AD). Although tau is a cytosolic microtubule …

Cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI)-anchored protein most
abundantly found in the outer membrane of neurons. Due to structural characteristics (a …

Conformational conversion of the α-helix-rich cellular prion protein into the misfolded, β-rich,
aggregated, scrapie form underlies the molecular basis of prion diseases that represent a …

Amyloid proteins are widely studied, both for their unusual biophysical properties and their
association with disorders such as Alzheimer's and Parkinson's disease. Fluorescence …

Aggregation of microtubule-associated protein Tau (MAPT) may underlie abnormalities of
the intracellular matrix and neuronal death in tauopathies. Tau proteins can be secreted to …

Cytoplasmic aggregation of the primarily nuclear TAR DNA-binding protein 43 (TDP-43)
affects neurons in most amyotrophic lateral sclerosis (ALS) and approximately half of …