L. Nagel-Steger

The paper studies glycine receptor intracellular domains using a pentameric scaffold, revealing structural flexibility and a mechanism for gephyrin clustering at inhibitory synapses.

This paper characterizes a small-molecule inhibitor of RUNX1/ETO tetramerization, showing it disrupts tetramer stability and has favorable pharmacokinetic properties for potential anti-leukemic therapy.

This study shows that all tested patient-derived immunoglobulin light chains have comparable amyloidogenic potential, with proteolytic cleavage being a key determinant of in vivo aggregation.