Alzheimer's disease is associated with the deposition of the amyloid-β peptide (Aβ) into
extracellular senile plaques in the brain. In vitro and in vivo observations have indicated that …

Abstract Characterization of small oligomers formed at an early stage of amyloid formation is
critical to understanding molecular mechanism of pathogenic aggregation process. Here we …

Transthyretin (TTR) aggregation via misfolding of a mutant or wild-type protein leads to
systemic or partial amyloidosis (ATTR). Here, we utilized variable biophysical assays to …

We have studied the intrinsic fluorescence spectra of a monomeric variant of human
transthyretin (M-TTR), a protein involved in the transport of the thyroid hormone and retinol …

Living systems protect themselves from aberrant proteins by a network of chaperones. We
have tested in vitro the effects of different concentrations, ranging from 0 to 16 μm, of two …

Human profilin-1 is a novel protein associated with a recently discovered form of familial
amyotrophic lateral sclerosis. This urges the characterization of possible conformational …

Src Homology 2 (SH2) domains are a class of protein domains that present a conserved
three‐dimensional structure and possess a crucial role in mediating protein‐protein …

An elastin-like polypeptide (ELP) was fused to d-amino acid oxidases (DAAO). ELP–DAAO
exhibited a better solubility in aqueous solutions than DAAO, and its enzymatic activity is …

Misfolding and aggregation of transthyretin (TTR) is widely known to be responsible for a
progressive systemic disorder called amyloid transthyretin (ATTR) amyloidosis. Studies …

Transthyretin (TTR) is an extracellular protein able to deposit into well-defined protein
aggregates called amyloid, in pathological conditions known as senile systemic …