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) …

Diagnosis of neurodegenerative disorders (NDDs) including Parkinson's disease and
Alzheimer's disease is challenging owing to the lack of tools to detect preclinical biomarkers …

Amyloid fibrils are insoluble, fibrous nanostructures that accumulate extracellularly in
biological tissue during the progression of several human disorders, including Alzheimer's …

Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely
instigators of neurodegeneration in Alzheimer's disease. We report results of time-resolved …

Soluble low-molecular-weight oligomers formed during the early aggregation of amyloid
peptides have been hypothesized as a major toxic species of amyloidogenesis. Herein, we …

Aβ aggregation leads to the formation of both insoluble amyloid fibrils and soluble
oligomers. Understanding the structures of Aβ oligomers is important for delineating the …

We present solid-state NMR measurements of β-strand secondary structure and inter-strand
organization within a 150-kDa oligomeric aggregate of the 42-residue variant of the …

Alzheimer's disease is characterized by the presence of distinct amyloid-β peptide (Aβ)
assemblies with diverse sizes, shapes, and toxicity. However, the primary determinants of …

Extracellular accumulation of β amyloid peptides of 40 (Aβ40) and 42 residues (Aβ42) has
been considered as one of the hallmarks in the pathology of Alzheimer's disease. In this …

Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid β (Aβ) protein
aggregates. Binding of Aβ oligomers to membrane-anchored huPrP has been suggested to …