Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …

Protein misfolding and amyloid assembly have long been recognized as being responsible
for many devastating human diseases. Recent findings indicate that amyloid assemblies …

Extensive studies indicate that β-amyloid (Aβ) aggregation is pivotal for Alzheimer's disease
(AD) progression; however, cumulative evidence suggests that Aβ itself is not sufficient to …

Although protein folding and stability have been well explored under simplified conditions in
vitro, it is yet unclear how these basic self-organization events are modulated by the …

Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …

Amyloid is aggregated protein in the form of insoluble fibrils. Amyloid deposition in human
tissue—amyloidosis—is associated with a number of diseases including all common …

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 …

Society is increasingly exposed to nanoparticles as they are ubiquitous in nature and
introduced as man-made air pollutants and as functional ingredients in cosmetic products as …

Amyloidosis refers to the extracellular tissue deposition of fibrils composed of low-molecular-
weight subunits of a variety of proteins. These deposits may result in a wide range of clinical …

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