The workshop on “Strategies and tools for modulating pathologic protein self-assembly" will join leading experts to discuss the current knowledge on the mechanisms underpinning self-assembly of disease-related proteins and present strategies to modulate toxic protein aggregation. Aberrant protein self-assembly is linked to over 30 human disorders, including neurodegenerative diseases, type-2 diabetes, and systemic amyloidosis. Misfolded and aggregated proteins also play a detrimental role in conditions in which clearance becomes deficient, such as lysosomal storage diseases. In addition, amyloid structures can be hijacked by viruses, e.g. HIV to increase infection. In all these conditions, a common characteristic of the proteins involved in the appearance of diverse, mostly non-native assemblies of the disease-related proteins, ranging from small oligomers to amyloid deposits. We have recently witnessed significant progress in understanding the biophysical and structural properties of these protein assemblies and in identifying their cytotoxicity mechanisms. These advances have been crucial to developing novel disease-modifying strategies and molecules. Despite this significant progress, we are still waiting for the appearance of the first effective drug designed to abrogate pathological protein self-assembly.