Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes.

C-terminal truncation of Îą-synuclein promotes amyloid fibril amplification at physiological pH.

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.

Optical Structural Analysis of Individual Îą-Synuclein Oligomers.

Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.

Biophotonics of Native Silk Fibrils.

Correction to 'Bifunctional fluorescent probes for detection of amyloid aggregates and reactive oxygen species'.

Microfluidic approaches for probing amyloid assembly and behaviour.

The small heat shock protein Hsp27 binds Îą-synuclein fibrils, preventing elongation and cytotoxicity.

Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity.

Microfluidic Diffusion Platform for Characterizing the Sizes of Lipid Vesicles and the Thermodynamics of Protein-Lipid Interactions.

Direct Observation of Oligomerization by Single Molecule Fluorescence Reveals a Multistep Aggregation Mechanism for the Yeast Prion Protein Ure2.

On-chip measurements of protein unfolding from direct observations of micron-scale diffusion.

Bifunctional fluorescent probes for detection of amyloid aggregates and reactive oxygen species.

Immunization with Îą-synuclein/Grp94 reshapes peripheral immunity and suppresses microgliosis in a chronic Parkinsonism model.