Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

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 …

Protein aggregation occurs as a consequence of perturbations in protein homeostasis that
can be triggered by environmental and cellular stresses. The accumulation of protein …

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

Acinetobacter baumannii is considered one of the most persistent pathogens responsible for
nosocomial infections. Due to the emergence of multidrug resistant strains, as well as high …

Transition of soluble proteins into insoluble amyloid fibrils is driven by self-propagating short
sequence stretches. However, accurate prediction of aggregation determinants remains …

The amyloid conformation can be adopted by a variety of sequences, but the precise
boundaries of amyloid sequence space are still unclear. The currently charted amyloid …

Decades of research into bacterial persistence has been unable to fully characterize this
antibiotic-tolerant phenotype, thereby hampering the development of therapies effective …

Functional amyloid is produced by many organisms but is particularly well understood in
bacteria, where proteins such as CsgA (E. coli) and FapC (Pseudomonas) are assembled as …

Facing the increasing occurrence of “big six” Escherichia coli outbreaks linked to fresh
produce, chlorine-based sanitisers are widely used for fresh produce decontamination in …