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 …

Protein aggregation is a widespread phenomenon with important implications in many
scientific areas. Although amyloid formation is typically considered as detrimental, functional …

Cryoelectron microscopy (cryo-EM) has provided unprecedented insights into amyloid fibril
structures, including those associated with disease. However, these structures represent the …

One of the hallmark pathologies of Alzheimer's disease (AD) is the presence of extracellular
deposits of diffuse and fibrillar amyloid plaques predominantly consisting of the amyloid-β …

Deposits of amyloid-β (Aβ) in the brains of rodents can be analysed by invasive intravital
microscopy on a submillimetre scale, or via whole-brain images from modalities lacking the …

The molecular architecture of amyloids formed in vivo can be interrogated using luminescent
conjugated oligothiophenes (LCOs), a unique class of amyloid dyes. When bound to …

Microglial dysfunction is a key pathological feature of Alzheimer's disease (AD), but little is
known about proteome-wide changes in microglia during the course of AD and their …

The accumulation of misfolded proteins (MP s), both unique and common, for different
diseases is central for many chronic degenerative diseases. In certain patients, MP …

Amyloid-β (Aβ) plaques, a hallmark of Alzheimer's disease (AD), are surrounded by regions
of neuronal and glial hyperactivity. We use in vivo two-photon and wide-field imaging of the …

Amyloid-β (Aβ) deposits are a relatively late consequence of Aβ aggregation in Alzheimer's
disease. When pathogenic Aβ seeds begin to form, propagate and spread is not known, nor …