An optogenetic approach has been developed to model Alzheimer's disease allowing light-induced Amyloid-β aggregation and tested in three model organisms, Drosophila, C. elegans and D. rerio.

Soluble amyloid-β precursor peptide has no functional effects at recombinant and native GABA_B receptors.

Altered coupling of different brain waves during sleep is associated with worse brain features related to Alzheimer’s disease processes and cognitive performance, suggesting that sleep brain waves coupling may contribute to poorer brain and cognitive trajectories in ageing.

The cyclic neuropeptide somatostatin binds to human Aβ1-42 through an interface that critically relies on a specific tryptophan, thereby blocking the propensity of Aβ to aggregate, a critical step in the pathobiology of Alzheimer's disease.

The role of amyloid-β-aggregation sequence and of the various domains in the physiological function of the FLO11-encoded adhesin in the yeast Saccharomyces cerevisiae are disclosed in this report.

Molecular genetics identifies a novel microglial pathway essential for mouse brain development and a previously unknown anti-inflammatory activity of monomeric amyloid β that activates this pathway.

Tau deposition in the aging brain follows patterns of functional connectivity that correspond to specific neural memory networks, and this relationship is strengthened in the presence of amyloid-β.

Monitoring the formation of two distinct arrangements in early amyloid-ß aggregation by mass spectrometry and ion mobility allows determination of the effect of potential drug candidates.

Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

Amyloid-β oligomers associated with Alzheimer’s disease interact with dynein motors to impair retrograde transport of autophagic vesicles in neurons.