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 …

The molecular details involved in the folding, dynamics, organization, and interaction of
proteins with other molecules are often difficult to assess by experimental techniques …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Stroke and Alzheimer's disease (AD) are cerebral pathologies with high socioeconomic
impact that can occur together and mutually interact. Vascular factors predisposing to …

To visualize amyloid β (Aβ) aggregates requires an uncontaminated and artifact-free
interface. This paper demonstrates the interface between graphene and pure water (verified …

The fibrillization and deposition of β‐amyloid protein (Aβ) are recognized to be the
pathological hallmarks of Alzheimer's disease (AD), which signify the need for the effective …

The structural polymorphism and the physiological and pathophysiological roles of two
important proteins, β-amyloid (Aβ) and tau, that play a key role in Alzheimer's disease (AD) …

The design of high-efficiency scavengers targeting β-amyloid protein (Aβ) plaques in the
progress of Alzheimer's disease (AD) has been recognized as an effective way to prevent …

A recently proposed lipid-chaperone hypothesis suggests that free lipid molecules, not
bound to membranes, affect the aggregation of amyloidogenic peptides such as amyloid-β …

β-Amyloid (Aβ) fibrillogenesis is closely associated with the pathogenesis of Alzheimer's
disease (AD), so detection and inhibition of Aβ aggregation are of significance for the …