Stefan Rüdiger

Fibril Paint: a class of amyloid-targeting peptides

This paper introduces FibrilPaints, a modular peptide system for selective amyloid binding and manipulation, showing that sequence variations affect binding affinity while allowing functional modifications.

FibrilPaints for visualisation and ubiquitination of Huntingtin amyloid fibrils

This paper introduces FibrilPaint peptides that selectively bind and track HttEx1Q44 amyloid fibrils, enabling monitoring of fibril growth and molecular targeting through ubiquitination.

Site-specific phosphorylation of Ser352 drives aggregation of Tau R4 under acidosis conditions

The paper identifies site-specific phosphorylation of Ser352 as the molecular switch driving Tau R4 aggregation under acidosis conditions.

The role of specific phosphorylation patterns in the oligomerization of Tau-R4

This study investigates how specific phosphorylation patterns affect the aggregation and condensation of the Tau-R4 domain using synthetic peptides.

Fibril fragmentation generates diversity in seed population

This study quantifies how ultrasound affects fibril fragmentation in patient-derived and recombinant fibrils from neurodegenerative diseases, showing that patient-derived fibrils fragment more easily.

FibrilPaint20 directs the ubiquitin-proteasome system to Tau amyloid fibrils

The paper demonstrates that FP20 recruits the ubiquitin-proteasome system to Tau amyloid fibrils, enabling their degradation and offering a strategy for targeting amyloid diseases.

Refolding activity of bacterial Hsp90 in vivo reveals ancient chaperoning function

This study shows that bacterial Hsp90 enhances protein refolding after heat stress but is not required for de novo folding, revealing its ancient role in the chaperone cascade.

Human chaperones untangle fibrils of the Alzheimer protein Tau

This study shows human Hsp70 chaperones can dissolve Tau fibrils, while bacterial Hsp70 systems cannot, suggesting evolutionary adaptation for fibril disaggregation and potential therapeutic applications for Alzheimer's.

Successful aggregation of Tau protein labelled on its native cysteines

This study shows that labelling Tau protein's native cysteines with large fluorescent dyes does not interfere with fibrillation, enabling structural analysis during the process.