Susanne Wegmann

Inhomogeneous Tau polymerization, core-shell organization, and seed formation during Tau condensate aging

This study shows how Tau condensates age into elastic networks with inhomogeneous polymerization and seed formation, providing mechanistic insight into their transition to pathological aggregates.

IgLON5 autoimmune antibodies activate Tau via neuronal hyperactivity

This study shows that IgLON5 autoantibodies cause neuronal hyperactivity and Tau pathology by clustering cell surface proteins, linking them to neurodegeneration.

Acute exposure of mouse and human hippocampal slices to tau oligomers reversibly impairs sharp-wave ripples

The paper investigates the effects of tau oligomers on sharp-wave ripples in mouse and human hippocampal slices, finding reversible impairments in SWR parameters depending on species and tau preparation.

A calcium imaging pipeline to detect and quantify compound-specific effects in human and mouse astrocytes and astrocyte-neuron cocultures

The paper develops a calcium imaging pipeline to assess compound effects on astrocyte activity in human and mouse cultures, finding differential responses to drugs and disease models.

Tau modulates nuclear integrity, chromatin, and cholesterol synthesis genes via the nuclear envelope

This study shows that increased somatodendritic Tau interacts with nuclear envelope proteins, causing nuclear damage and altering gene expression related to AD and tauopathies.

Membrane protein condensates polymerize actin and form filopodia

This study identifies PLPPR3 condensates as actin sinks that locally boost monomer concentrations, promoting actin polymerization and filopodia formation in neurons.

Stoichiometric 14-3-3ζ binding promotes phospho-Tau microtubule dissociation and reduces aggregation and condensation

This study shows that 14-3-3ζ binding to phosphorylated Tau reduces its association with microtubules and inhibits aggregation and condensation.

Direct binding of TDP-43 and Tau drives their co-condensation, but suppresses Tau fibril formation and seeding

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

Biomolecular Tau condensation is linked to Tau accumulation at the nuclear envelope

This study shows that Tau condensation, driven by molecular crowding and RNA coacervation, leads to pathological Tau accumulation at the nuclear envelope and affects nucleocytoplasmic transport.