Kinetic diversity of amyloid oligomers.

Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform.

The Influence of Pathogenic Mutations in Îą-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils.

Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.

A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation.

Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers.

ThX - a next-generation probe for the early detection of amyloid aggregates.

The Amyloid Phenomenon and Its Significance in Biology and Medicine.

A Role of Cholesterol in Modulating the Binding of Îą-Synuclein to Synaptic-Like Vesicles.

Correction: Defining Îą-synuclein species responsible for Parkinson's disease phenotypes in mice.

Proteome-wide observation of the phenomenon of life on the edge of solubility.

The N-terminal Acetylation of Îą-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State.

Lipid Dynamics and Phase Transition within Îą-Synuclein Amyloid Fibrils.

A metastable subproteome underlies inclusion formation in muscle proteinopathies.