Misfolding and aggregation of peptides and proteins is a characteristic of many
neurodegenerative disorders, including Alzheimer's disease (AD). In AD the β-amyloid …

The self-assembly of normally soluble proteins into fibrillar amyloid structures is associated
with a range of neurodegenerative disorders, such as Parkinson's and Alzheimer's diseases …

Deposition of amyloid β (Aβ) fibrils has been suggested to play a central role in Alzheimer's
disease. In clarifying the mechanism by which fibrils form and moreover in developing new …

Insight into how amyloid β (Aβ) aggregation occurs in vivo is vital for understanding the
molecular pathways that underlie Alzheimer's disease and requires new techniques that …

The misfolding and aggregation of proteins into amyloid fibrils characterizes many
neurodegenerative disorders such as Parkinson's and Alzheimer's diseases. We report here …

The progressive deposition of the amyloid β peptide (Aβ) in fibrillar form is a key feature in
the development of the pathology in Alzheimer's disease (AD). We have characterized the …

Protein misfolding into amyloid-like aggregates underlies many neurodegenerative
diseases. Thus, insights into the structure and function of these amyloids will provide …

Evidence suggests that oligomers of the 42-residue form of the amyloid β-protein (Aβ), Aβ42,
play a critical role in the etiology of Alzheimer's disease (AD). Here we use high resolution …

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

The misfolding and self-assembly of intrinsically disordered proteins into insoluble amyloid
structures are central to many neurodegenerative diseases such as Alzheimer's and …