Recent studies suggest that deposition of amyloid β (Aβ) into oligomeric aggregates and
fibrils, hallmarks of Alzheimer's disease, may be initiated by the aggregation of Aβ species …

A mechanistic understanding of Aβ aggregation and high-resolution structures of Aβ fibrils
and oligomers are vital to elucidating relevant details of neurodegeneration in Alzheimer's …

Recently, certain C-terminal fragments (CTFs) of Aβ42 have been shown to be effective
inhibitors of Aβ42 toxicity. Here, we examine the interactions between the shortest CTF in …

Aggregation of the amyloid-β (Aβ) peptide into plaques is believed to play a crucial role in
Alzheimer's disease. Amyloid plaques consist of fibrils of full length Aβ peptides as well as N …

Aβ40 and Aβ42 are the predominant Aβ species in the human body. Toxic Aβ42 oligomers
and fibrils are believed to play a key role in causing Alzheimer's disease (AD). However, the …

A key event in Alzheimer's disease (AD) is age-dependent, brain accumulation of amyloid β-
protein (Aβ) leading to Aβ self-association into neurotoxic oligomers. Previously, we showed …

Oligomeric forms of amyloid β-protein (Aβ) are key neurotoxins in Alzheimer's disease (AD).
Previously, we found that C-terminal fragments (CTFs) of Aβ42 interfered with assembly of …

Aβ40 and Aβ42 are the major forms of amyloid β peptides (Aβ) in the brain. Although Aβ42
differs from Aβ40 by only two residues, Aβ42 is much more prone to aggregation and more …

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 …

Soluble oligomers and protofibrils of the Aβ42 peptide are neurotoxic intermediates in the
conversion of monomeric Aβ42 into the amyloid fibrils associated with Alzheimer's disease …