Markus Zweckstetter

This paper investigates how environmental conditions influence the structural assembly and cytotoxic function of the Staphylococcus aureus virulence peptide PSM1, revealing condition-dependent polymorphic structures and their role in host-cell interactions.

The paper shows that ERK2 phosphorylation of tau outside the amyloid core directs fibril formation into an Alzheimer's disease-like structure.

The paper shows RNA modulates assembly and activity of two -helical peptides, PSM3 and LL-37, through phase separation and aggregation dynamics, affecting virulence and host defense.

The paper investigates how a disease-associated TSPO variant affects transmembrane helix dynamics using solution NMR spectroscopy.

This study investigates how Tau and Fyn interact to regulate postsynaptic density condensate dynamics, showing that their multivalent interactions cooperatively arrest condensate components.

AI-IDP predicts conformational ensembles of disordered proteins by combining deep learning with physical restraints, revealing common structural features across proteomes.

This study shows that PPM1H knockout disrupts axonal autophagy and increases alpha-synuclein aggregation in neurons, linking LRRK2 hyperactivity to Parkinson disease pathology.

This paper designs a synthetic peptide mimicking Hsp90-Tau interaction to inhibit Tau aggregation and restore its microtubule binding, showing efficacy in vitro and in cells.

This study shows that TDP-43 and Tau directly interact, promoting co-condensation but reducing Tau fibril formation and seeding.

The paper investigates the role of oligodendroglial-derived extracellular vesicles in spreading pathology in MSA-like models, showing they carry pathological Synuclein and TPPP/p25 and induce disease in animal models.

This study shows polyamines promote disordered protein phase separation by interacting with acidic domains and modulate amyloid formation in Parkinson's disease-related proteins.

This study investigates RNA polymerase II condensates in C. elegans using simulations and experiments, showing they exhibit LCST behavior and form distinct phases during transcription.

The paper investigates the effects of the E83Q mutation on alpha-synuclein aggregation and toxicity, finding it accelerates fibrillization and enhances pathological features in neuronal models.

This study compares the release and effects of alpha-synuclein, Tau, and huntingtin in neuronal cells, showing similar release pathways and impacts on neuronal activity and inflammation.

This study compares α-synuclein fibril structures from Parkinson's disease and Multiple System Atrophy patients, showing differences in their quaternary arrangement and effects on oligodendroglial cells.

The paper evaluates pharmacological modulators of α-synuclein and tau aggregation and internalization, identifying compounds that reduce their aggregation and spread.

The paper develops a fluorescent reporter (FluoReSyn) using a nanobody to detect human α-synuclein in cells and tissues, showing its presence in cerebrospinal fluid.

This study shows that RNA polymerase II CTDs undergo phase separation, forming clusters that are regulated by phosphorylation and CTD length.