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 …

Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

Aggregation of alpha-synuclein (α-Syn) drives Parkinson's disease (PD), although the initial
stages of self-assembly and structural conversion have not been directly observed inside …

Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

To date, no reliable clinically applicable biomarker has been established for Parkinson's
disease. Our results indicate that a long anticipated blood test for Parkinson's disease may …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Soluble α-synuclein aggregates varying in size, structure, and morphology have been
closely linked to neuronal death in Parkinson's disease. However, the heterogeneity of …

Oligomeric species populated during the aggregation process of α-synuclein have been
linked to neuronal impairment in Parkinson's disease and related neurodegenerative …

According to emerging studies, the excessive activation of microglia and the subsequent
release of pro-inflammatory cytokines play important roles in the pathogenesis and …

Neurodegenerative diseases pose a substantial socioeconomic burden on society.
Unfortunately, the aging world population and lack of effective cures foreshadow a negative …