The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from
proteins associated with different diseases remains unclear. Here, we combine cryo-EM and …

Crystals, nanoparticles, and fibrils catalyze the generation of new aggregates on their
surface from the same type of monomeric building blocks as the parent assemblies. This …

Electrostatic interactions play crucial roles in protein function. Measuring p K a value
perturbations upon complex formation or self-assembly of eg amyloid fibrils gives valuable …

The pathology of Alzheimer's disease is connected to the aggregation of β-amyloid (Aβ)
peptide, which in vivo exists as a number of length-variants. Truncations and extensions are …

Aberrant soluble oligomers formed by the amyloid-β peptide (Aβ) are major pathogenic
agents in the onset and progression of Alzheimer's disease. A variety of biomolecules can …

The major hallmark of Alzheimer's disease is the deposition of plaques of amyloid fibrils
formed from amyloid-β (Aβ) peptides. Kinetic studies have contributed significantly towards a …

Structural differences in pathological and functional amyloid fibrils have been investigated
by Raman microspectroscopy. Second-derivative analyses of amide-I and amide-III bands …

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 …

Several publications describing high-resolution structures of amyloid-β (Aβ) and other fibrils
have demonstrated that magic-angle spinning (MAS) NMR spectroscopy is an ideal tool for …