The phenomenon of protein aggregation into amyloid fibrils is associated with a large
number of major diseases of unrelated etiology. Unraveling the mechanism of amyloid self …

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Protein misfolding into amyloid fibrils is linked to more than 40 as yet incurable cell‐and
neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and type 2 …

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

The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …

Self-assembly of proteins into amyloid fibrils plays a key role in a multitude of human
disorders that range from Alzheimer's disease to type II diabetes. Compact oligomeric …

Many proteins of diverse sequence, structure and function self-assemble into
morphologically similar fibrillar aggregates known as amyloids. Amyloids are remarkable …

The aggregation of proteins and peptides in the form of stable and highly ordered amyloid
fibrils is most commonly associated with pathological conditions such as Alzheimer's …

Functional amyloids are a rapidly expanding class of fibrillar protein structures, with a core
cross-β scaffold, where novel and advantageous biological function is generated by the …

Amyloids were first identified in association with amyloidoses, human diseases in which
proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an …