Abnormal assembly of tau, α-synuclein, TDP-43 and amyloid-β proteins into amyloid
filaments defines most human neurodegenerative diseases. Genetics provides a direct link …

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 …

Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-
β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's …

The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer's disease
and cerebral amyloid angiopathy. However, the structure of Aβ amyloid fibrils from brain …

Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the
pathogenesis of Alzheimer's disease. Fibrils formed in vitro by 40-and 42-residue amyloid-β …

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that
depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here …

We describe the isolation and detailed structural characterization of stable toxic oligomers of
α-synuclein that have accumulated during the process of amyloid formation. Our approach …

This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

The cross-β amyloid form of peptides and proteins represents an archetypal and widely
accessible structure consisting of ordered arrays of β-sheet filaments. These complex …

Progressive cerebral deposition of the amyloid β-protein (Aβ) in brain regions serving
memory and cognition is an invariant and defining feature of Alzheimer disease. A highly …