G. P. Liszczak

The paper develops an MS-based workflow to detect Glu/Asp-ADPr modifications, identifies over 600 sites in cytokine-stimulated cells, and reveals residue-specific ADPr dynamics in immune signaling.

The paper uses chiral inversion mutagenesis to identify geometrically constrained residues in LCDs that affect self-association.

The paper identifies the ETS domain as a structure-encoded NLS recognized by importins, revealing how importins mediate nuclear import of ETS transcription factors.

The paper describes a method to identify cross-β forming regions in low complexity domains that mediate self-association and phase separation.

The paper identifies missense mutations that create nuclear export signals, leading to disease, and shows therapeutic strategies can restore function.