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 …

Amyloid proteins, which are considered 'villains' in many neurodegenerative diseases, form
enigmatic pathological strains that underlie disease pathogenesis and progression. Recent …

Hereditary transthyretin amyloidosis (ATTRv) is a severe, adult-onset autosomal dominant
inherited systemic disease predominantly affecting the peripheral and autonomic nervous …

Amyloid-forming proteins such α-synuclein and tau, which are implicated in Alzheimer's and
Parkinson's disease, can form different fibril structures or strains with distinct toxic properties …

Scientific advances over the last four decades have steadily infused the Alzheimer's disease
(AD) field with great optimism that therapies targeting Aβ, amyloid, tau, and innate immune …

In most cases, protein aggregation stems from the establishment of non-native
intermolecular contacts. The formation of insoluble protein aggregates is associated with …

The spread of pathological α-synuclein (α-syn) is a crucial event in the progression of
Parkinson's disease (PD). Cell surface receptors such as lymphocyte activation gene 3 …

Amyloid aggregation, which disrupts protein homeostasis, is a common pathological event
occurring in human neurodegenerative diseases (NDs). Numerous evidences have shown …

Protein aggregation is a widespread phenomenon with important implications in many
scientific areas. Although amyloid formation is typically considered as detrimental, functional …

Abstract α-Synuclein forms amyloid fibrils that are critical in the progression of Parkinson's
disease and serves as the pathological hallmark of this condition. Different posttranslational …