Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …

Background The global rise of metabolic disorders, such as obesity, type 2 diabetes, and
cardiovascular disease, demands a thorough molecular understanding of the cellular …

Nature programs the structural folding of an enzyme that allows its on-demand
biofunctionality; however, it is still a long-standing challenge to manually modulate an …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

The endoplasmic reticulum (ER) is a large, dynamic structure that serves many roles in the
cell including calcium storage, protein synthesis and lipid metabolism. The diverse functions …

A hallmark of neurodegenerative proteinopathies is the formation of misfolded protein
aggregates that cause cellular toxicity and contribute to cellular proteostatic collapse …

The phenomenon of protein aggregation in food science is very common, but the formation
mechanism is unclear. The formation of protein aggregates (PAs) is influenced by various …

Accumulation of toxic protein aggregates—amyloid-β (Aβ) plaques and
hyperphosphorylated tau tangles—is the pathological hallmark of Alzheimer disease (AD) …

Biochemical processes take place in heterogeneous and highly volume-occupied or
crowded environments that can considerably influence the reactivity and distribution of …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …