Structural Characteristics of Îą-Synuclein Oligomers.

Multi-dimensional super-resolution imaging enables surface hydrophobicity mapping.

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.

Bifunctional Anti-Non-Amyloid Component Îą-Synuclein Nanobodies Are Protective In Situ.

β-Synuclein suppresses both the initiation and amplification steps of ι-synuclein aggregation via competitive binding to surfaces.

Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.

Structural basis of synaptic vesicle assembly promoted by Îą-synuclein.

The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity.

Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of Îą-synuclein aggregation.

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.

Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies.

Physical determinants of the self-replication of protein fibrils.

A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease.

Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.

Towards a structural biology of the hydrophobic effect in protein folding.