David Bernson

2024

Extracellular Vesicles Slow Down Aβ(1-42) Aggregation by Interfering with the Amyloid Fibril Elongation Step

2020

Amyloid formation of bovine insulin is retarded in moderately acidic pH and by addition of short-chain alcohols

Correlation between Cellular Uptake and Cytotoxicity of Fragmented α-Synuclein Amyloid Fibrils Suggests Intracellular Basis for Toxicity

2020

Graphene oxide sheets and quantum dots inhibit alpha-synuclein amyloid formation by different mechanisms

2020

Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro

2020

Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers

Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42)

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

Amyloid Fibril Formation - Dye Detection and Effects of Lipids

Lipid membranes catalyse the fibril formation of the amyloid-? (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways

Detection of amyloid-beta fibrils using the DNA-intercalating dye YOYO-1: Binding mode and fibril formation kinetics

2015

Steady-state and time-resolved Thioflavin-T fluorescence can report on morphological differences in amyloid fibrils formed by A beta(1-40) and A beta(1-42)

Time-resolved thioflavin-T fluorescence-expanding the amyloid characterisation toolbox

2015

Development of the Amyloid Fibril Characterisation Toolbox - New use for old dyes

Vortex matter in Bi2Sr2CaCu2O8+x with controlled interlayer coupling