Recombinant proteins are becoming increasingly important for industrial applications, where
Escherichia coli is the most widely used bacterial host for their production. However, the …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Self-assembling systems play a significant role in physiological functions and have therefore
attracted tremendous attention due to their great potential for applications in energy …

Protein instability caused by exposure to external additives or severe stress may result in
different diseases. Of these diseases, many are triggered by protein misfolding and …

Protein aggregation has been recognized as one of the major challenges in the
development and commercialization of successful protein-based drug products because of …

Aggregation of amyloid-β (Aβ) by self-assembly into oligomers or amyloids is a central event
in Alzheimer's disease. Coordination of transition-metal ions, mainly copper and zinc, to Aβ …

The maintenance of protein solubility is a fundamental aspect of cellular homeostasis
because protein aggregation is associated with a wide variety of human diseases …

Our understanding of cells has progressed rapidly in recent years, mainly because of
technological advances. Modern technology now allows us to observe molecular processes …

Amyloid fibrils are supramolecular protein assemblies with a fibrous morphology and cross-
β structure. The formation of amyloid fibrils typically follows a nucleation-dependent …

Amyloid fibrils are self‐assembled fibrous protein aggregates that are associated with a
number of presently incurable diseases such as Alzheimer's and Parkinson's disease …