Katja Bernfur

Errors in peptide synthesis are a source of discrepancies in Aβ42 studies

This study shows that sequence imperfections in synthetic Aβ42 peptides cause differences in aggregation behavior compared to recombinant Aβ42.

Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15

This study shows that PARP15's ADP-ribosyltransferase activity is regulated by dimerization, with dimers required for catalytic function and monomers inactive.

On the transient interactions of α-synuclein in different dimensions

This study uses PICUP to identify transient α-synuclein contacts in different conformational states, revealing state-specific interactions in solution, membrane-bound, and fibril forms.

Tipping point in α-synuclein-membrane interactions: stable protein-covered vesicles or amyloid aggregation

This study investigates how lipid membranes influence the equilibrium between free and membrane-bound α-synuclein and its amyloid formation, revealing conditions that promote or inhibit aggregation.

The bacterial amyloids phenol soluble modulins from Staphylococcus aureus catalyze alpha-synuclein aggregation

This study shows that Staphylococcus aureus PSM peptides catalyze alpha-synuclein aggregation, potentially linking the microbiome to Parkinson's disease pathology.

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

This study investigates the dynamics of Aβ42 oligomers during amyloid fibril formation, revealing that most oligomers dissociate into monomers rather than forming fibrils.

Kinetic fingerprints differentiate anti-Aβ therapies

This study uses kinetic analysis and binding measurements to compare four anti-Aβ antibodies, showing aducanumab uniquely reduces Aβ oligomer flux.