Rita Pancsa

This study identifies extracellular regions and human-pathogen interaction interfaces as hotspots of positive selection in human proteins.

This paper reports on the fourth CAFA challenge, showing improvements in Gene Ontology term prediction but highlighting challenges in new evaluation settings.

This study identifies the RNA-binding region of the androgen receptor and shows how lncRNA binding modulates interdomain communication and phase separation, contributing to ligand-independent AR signaling in prostate cancer.

The paper develops SLiMMine, a deep learning method to predict short linear motifs in the human proteome with reduced false positives and the ability to discover novel motifs.

The paper defines the binding preference of tandem SH3 domains in p47phox-related proteins and identifies potential new instances through integrative analysis and structure prediction.

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.

This study shows that C9orf72-derived arginine-rich dipeptide repeats enhance G3BP1 phase separation, contributing to ALS and FTD pathology.

The paper identifies charged sequence motifs in proteins that are associated with liquid-liquid phase separation, with alternating charge patterns showing the strongest association.

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 examines the concentration sensitivity of proteins involved in liquid-liquid phase separation and argues that in vitro concentrations are reasonable given cellular dosage sensitivity.

The paper introduces a method to study liquid-liquid phase separation under near-native conditions by using extreme pH to control protein solubility and induce phase separation.