When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-
sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are …

Amyloid is a distinct β-sheet-rich fold that many proteins can acquire. Frequently associated
with neurodegenerative diseases in humans, including Alzheimer's, Parkinson's and …

Amyloids are a class of protein with unique self-aggregation properties, and their aberrant
accumulation can lead to cellular dysfunctions associated with neurodegenerative diseases …

Protein aggregation results in β-sheet–like assemblies that adopt either a variety of
amorphous morphologies or ordered amyloid-like structures. These differences in structure …

Many bacteria assemble extracellular amyloid fibers on their cell surface. Secretion of
proteins across membranes and the assembly of complex macromolecular structures must …

Amyloids are highly abundant in many microbial biofilms and may play an important role in
their architecture. Nevertheless, little is known of the amyloid proteins. We report the …

Protein aggregation and amyloid formation have historically been linked with various
diseases such as Alzheimer's and Parkinson's disease, but recently functional amyloids …

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 …

The fap operon, encoding functional amyloids in P seudomonas (Fap), is present in most
pseudomonads, but so far the expression and importance for biofilm formation has only …

Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and
contribute to biofilm formation, thereby promoting bacterial resistance to environmental …