Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Vaccines have had a profound impact on the management and prevention of infectious
disease. In addition, the development of vaccines against chronic diseases has attracted …

The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

The amyloid-β oligomer (AβO) hypothesis was introduced in 1998. It proposed that the brain
damage leading to Alzheimer's disease (AD) was instigated by soluble, ligand-like AβOs …

Most neurodegenerative diseases are proteinopathies, which are characterized by the
aggregation of misfolded proteins. Although many proteins have an intrinsic propensity to …

The amino-acid sequence of a protein encodes information on its three-dimensional
structure and specific functionality. De novo design has emerged as a method to manipulate …

Advances over the past 25 years have revealed much about how the structural properties of
membranes and associated proteins are linked to the thermodynamics and kinetics of …

Formation of amyloid-beta (Aβ) oligomer pores in the membrane of neurons has been
proposed to explain neurotoxicity in Alzheimerʼs disease (AD). Here, we present the three …

Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

It is widely accepted that β-amyloid oligomers (Aβos) play a key role in the progression of
Alzheimer's disease (AD) by inducing neuron damage and cognitive impairment, but Aβos …