Sean M. Cascarina

MatchIDR identifies prion-like domains that localize to stress granules by finding compositional matches in proteomes.

The paper identifies low-complexity domains (LCDs) across reference proteomes, revealing class-specific frequencies and functions, with many LCDs being eukaryote-specific.

The paper examines how the secondary structure preferences of low-complexity domains (LCDs) vary based on amino acid composition and enrichment, revealing distinct structural tendencies among LCDs with similar physicochemical properties.

The paper examines how sequence variation in prion-like domains (PrLDs) affects aggregation propensity in human proteins, identifying mutations linked to increased aggregation and disease.

The paper investigates how local amino acid composition influences protein metabolism, localization, and function across the proteome, revealing distinct effects based on amino acid type.