This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

Oligomeric intermediates are non-fibrillar polypeptide assemblies that occur during amyloid
fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as …

The oligomers formed during the early steps of amyloid aggregation are thought to be
responsible for the neurotoxic damage associated with Alzheimer's disease. It is therefore of …

Alzheimer's disease (AD) is a complex age‐related neurodegenerative disease. In this
review, we carefully detail amyloid‐β metabolism and its role in AD. We also consider the …

Copper is a redox-active metal with many important biological roles. Consequently, its
distribution and oxidation state are subject to stringent regulation. A large body of …

1. Introduction 22. What is the significance of the shared structural properties of disease-
associated protein fibrils? 32.1 Mechanism of amyloid fibril formation in vitro 62.1. 1 In vitro …

Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …

Amyloid fibrils are associated with a number of neurodegenerative diseases, including fibrils
of amyloid β42 peptide (Aβ42) in Alzheimer's disease. These fibrils are a source of toxicity to …

Previously, we have studied the minimal oligomer size of an aggregate amyloid seed and
the mechanism of seed growth with a multilayer β-sheet model. Under high temperature …

Experimental findings suggest that oligomeric forms of the amyloid β protein (Aβ) play a
critical role in Alzheimer's disease. Thus, elucidating their structure and the mechanisms of …