Transthyretin (TTR) is a protein linked to a number of different amyloid diseases including
senile systemic amyloidosis and familial amyloidotic polyneuropathy. The transient nature of …

We have revisited the well-studied heat and acidic amyloid fibril formation pathway (pH 1.6,
65 C) of hen egg-white lysozyme (HEWL) to map the barriers of the misfolding and …

Alzheimer disease (AD) is biochemically characterized by increased levels of amyloid β (Aβ)
peptide, which aggregates into extracellular Aβ plaques in AD brains. Before plaque …

Background Insulin-derived amyloidosis is a skin-related complication of insulin therapy that
interferes with insulin therapy. Although toxicities of in vitro-formed insulin amyloid fibrils …

Amyloid-β (Aβ) peptides represent key players in the pathogenesis of Alzheimer’s disease (AD),
and mounting evidence indicates that soluble Aβ oligomers mediate the toxicity. …

Amyloid beta (Aβ) peptides produced by APP cleavage are central to the pathology of
Alzheimer’s disease. Despite widespread interest in this issue, the relationship between the auto-…

Recent studies suggest that soluble, oligomeric species, which are intermediates in the fibril
formation process in amyloid disease, might be the key species in amyloid pathogenesis. …

Huntington disease is caused by cell death after the expansion of polyglutamine (polyQ)
tracts longer than ∼40 repeats encoded by exon 1 of the huntingtin (HTT) gene. Prefoldin is a …

Carriers of the D18G transthyretin (TTR) mutation display an unusual central nervous system
(CNS) phenotype with late onset of disease. D18G TTR is monomeric and highly prone to …

Needles and noodles: Studying amyloid toxicity is important for understanding protein misfolding
diseases. Using a luminescent conjugated polythiophene, we found that cell binding of …