The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that
depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here …

How long-lived memories withstand molecular turnover is a fundamental question.
Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element …

Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …

The development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various
neurodegenerative diseases. This process involves protein assembly into oligomeric …

As our understanding of the molecular structures of amyloid fibrils has matured over the past
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …

The intrinsically disordered protein tau associates with microtubules in neurons but
aggregates into cross–β amyloid fibrils that propagate in neurodegenerative brains. Different …

Protein domains without the usual distribution of amino acids, called low complexity (LC)
domains, can be prone to self-assembly into amyloid-like fibrils. Self-assembly of LC …