Understanding the mechanisms underlying protein misfolding and aggregation has become
a central issue in biology and medicine. Compelling evidence show that the formation of …

Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …

Protein aggregation serves as a critical pathological marker in a spectrum of
neurodegenerative diseases (NDs), including the formation of amyloid β (Aβ) and Tau …

An increasing number of human diseases has been shown to be linked to aggregation and
amyloid formation by intrinsically disordered proteins (IDPs). Amylin, amyloid-β, and α …

Atypical amyloid generation, folding, aggregation and impaired clearance are characteristic
pathological features of human neurodegenerative disorders including Alzheimer's disease …

Since the inception of the human microbiome project (HMP) by the US National Institutes of
Health (NIH) in 2007 there has been a keen resurgence in our recognition of the human …

According to the 'amyloid cascade hypothesis of Alzheimer's disease'first proposed about 16
years ago, the accumulation of Aβ peptides in the human central nervous system (CNS) is …

Small heat-shock proteins, including αB-crystallin (αB), play an important part in protein
homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled …

The green tea compound epigallocatechin-3-gallate (EGCG) inhibits Alzheimer's disease β-
amyloid peptide (Aβ) neurotoxicity. Solution-state NMR allows probing initial EGCG–Aβ …

In Alzheimer's disease, neurons slowly degenerate due to the accumulation of misfolded
amyloid β and tau proteins. In our research, we performed extended studies directed at …