1. Introduction 22. Sources of structural information in solid-state NMR data 52.1 General
remarks 52.2 Chemical shifts, linewidths, and magic-angle spinning 62.3 Dipole–dipole …

This review is focused on the structure and function of Alzheimer's amyloid deposits.
Amyloid formation is a process in which normal well-folded cellular proteins undergo a self …

We present a structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide
associated with Alzheimer's disease (Aβ1–40), based on a set of experimental constraints …

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 …

The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22
and representing residues 16− 22 of the full-length β-amyloid peptide associated with …

In general, proteins can only execute their various biological functions when they are
appropriately folded. Their amino acid sequence encodes the relevant information required …

Senile plaques associated with Alzheimer's disease contain deposits of fibrils formed by 39-
to 43-residue β-amyloid peptides with possible neurotoxic effects. X-ray diffraction …

Neurotoxic assemblies of the amyloid β‐protein (Aβ) have been linked strongly to the
pathogenesis of Alzheimer's disease (AD). Here, we sought to monitor the earliest step in Aβ …

We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-
residue β-amyloid peptide associated with Alzheimer's disease (Aβ 1–40) obtained from …

We describe electron microscopy (EM), scanning transmission electron microscopy (STEM),
and solid-state nuclear magnetic resonance (NMR) measurements on amyloid fibrils formed …