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The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity

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The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity

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Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches

Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

Multidimensional View of Amyloid Fibril Nucleation in Atomistic Detail

Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation

Self-Assembly of ß-Amyloid Peptides in Cells and on Solid Supports

Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species

Bloch Surface Wave Biosensing

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity

Fibrillar vs Crystalline Full-Length beta-2-Microglobulin Studied by High-Resolution Solid-State NMR Spectroscopy

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images