F.-U. Hartl

This study shows autophagosomes preferentially degrade non-fibrillar polyQ aggregates by interacting with p62, while amyloid fibrils evade clearance due to their non-deformable structure.

This paper introduces smMDS, a method for digital sizing of proteins in solution, enabling sensitive and accurate measurement of protein sizes and interactions.

This study identifies a NF-κB-independent role of NEMO in proteostasis by promoting aggrephagy through co-condensation with p62.

This study uses HDX-MS to map the cotranslational folding pathway of E. coli dihydrofolate reductase, revealing structured intermediates and chaperone interactions on the ribosome.

This study shows that the AAA+ chaperone VCP disaggregates Tau fibrils and generates seeding-active Tau as a byproduct, suggesting a role in aggregate removal and spreading in tauopathies.

This study shows the Hsc70-DnaJB1-Apg2 chaperone system removes monomer units directly from α-synuclein fibril ends, reversing aggregation without intermediate fragmentation.

This study compares the toxicity of C9orf72 DPRs and G4C2 RNA in a cellular model, finding that RNA has a more dominant toxic effect while DPRs add to pathology.