Bálint Mészáros

The paper identifies oncogenic fusion proteins that drive cancer by forming ectopic condensates that dysregulate transcription.

This paper shows that SMAUG1 forms condensates via its disordered region and that 14-3-3 proteins dissolve these condensates through phospho-regulated interactions.

PSINDB compiles postsynaptic protein-protein interactions with structural and biological details, providing a resource for neurobiology research.

The paper evaluates 43 methods for predicting intrinsically disordered regions and binding regions in proteins, finding that deep learning methods outperform older physicochemical approaches but binding prediction remains challenging.

The paper analyzes disease-causing germline mutations in coiled-coil structures and finds that N-terminal residues are critical for superhelix assembly and folding.

The paper identifies that mutations in intrinsically disordered regions (IDRs) are a distinct class of cancer drivers with unique functional mechanisms and therapeutic implications.

The paper identifies redox-sensitive conditionally disordered protein regions across proteomes and links their prevalence to biological processes and disease.

The paper identifies conserved SQ and QS motifs in bacterial effectors that may mimic ATM kinase substrates, suggesting a mechanism by which pathogens modulate host signaling during infection.

The paper identifies three scenarios of folding-binding interplay in IDPs, showing how binding partner properties influence protein sequence, structure, function, and regulation as much as inherent disorder.