Low pH has a strong stabilising effect on the fibrillar assembly of amyloid β, which is
associated with Alzheimer's disease. The stabilising effect is already pronounced at pH 6.0 …

Although the amyloid fibrils formed from the Alzheimer's disease amyloid peptide Aβ are rich
in cross-β sheet, the peptide likely also exhibits turn and unstructured regions when it …

We describe solid-state nuclear magnetic resonance (NMR) measurements on fibrils formed
by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1-40) that …

A key pathological feature of Alzheimer's disease (AD) is the formation and accumulation of
amyloid fibers within the neurophil as senile plaques and in the walls of cerebral and …

Proteins adopt an amazing array of sequence-dependent struc-tures that enable them to
perform the many chemical functions critical to life. Over the past decade, however, it has …

Protofibrils are transient structures observed during in vitro formation of mature amyloid
fibrils and have been implicated as the toxic species responsible for cell dysfunction and …

A signature feature of Alzheimer's disease is the accumulation of plaques, composed of
fibrillar amyloid-β protein (Aβ), in the brain parenchyma. Structural models of Aβ fibrils reveal …

To understand the molecular interactions leading to the assembly of beta/44 protein into the
hallmark fibrils of Alzheimer's disease (AD), we have examined the ability of synthetic …

In a recent model of β-amyloid (Aβ) fibrils, based mainly on solid-state NMR data, a
molecular layer consists of two β-sheets (residues 12− 23 and 31− 40 of Aβ1− 40), folded …

Protein− protein interactions are frequently mediated by stable, intermolecular β-sheets. A
number of cytokines and the HIV Protease, for example, dimerize through β-sheet motifs …