Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …

Amyloid-β (Aβ) is present in humans as a 39-to 42-amino acid residue metabolic product of
the amyloid precursor protein. Although the two predominant forms, Aβ (1–40) and Aβ (1 …

Alzheimer's disease is the most fatal neurodegenerative disorder wherein the process of
amyloid-β (Aβ) amyloidogenesis appears causative. Here, we present the 3D structure of the …

Understanding the molecular structures of amyloid-β (Aβ) oligomers and underlying
assembly pathways will advance our understanding of Alzheimer's disease (AD) at the …

Amyloid-beta (Aβ) aggregates are the main constituent of senile plaques, the histological
hallmark of Alzheimer's disease. Aβ molecules form β-sheet containing structures that …

We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-
residue β-amyloid peptide associated with Alzheimer's disease (Aβ 1–40) obtained from …

Fibrils formed by the 42-residue amyloid-β peptide (Aβ42), a main component of amyloid
deposits in Alzheimer's disease (AD), are known to be polymorphic, ie, to contain multiple …

We describe a full structural model for amyloid fibrils formed by the 40-residue β-amyloid
peptide associated with Alzheimer's disease (Aβ1–40), based on numerous constraints from …

Amyloid β (Aβ) peptides are a primary component of fibrils and oligomers implicated in the
etiology of Alzheimer's disease (AD). However, the intrinsic flexibility of these peptides has …

The amyloid fibrils of beta-amyloid (Aβ) peptides play important roles in the pathology of
Alzheimer's disease. Comprehensive solid-state NMR (SSNMR) structural studies on …