Our main interest is to the study the structural and functional properties of intrinsically disordered proteins and their involvement in various diseases. We develop various computational tools to aid research in this field, including prediction tools (e.g. IUPred and IUPred2A, ANCHOR) and databases (e.g. DIBS, PhaSePro). As many disordered proteins function through short linear motifs, we are also interested in how such functional sites can be identified from the amino acid sequence. We also study specific linear motif systems using a combination of computational and experimental methods. In particular, we are exploring the interaction partners of the dynein light chain LC8, and specific E3 ligases, such as SIAH.

Selected publications


IUPred2A: Prediction of Intrinsically Unstructured Proteins
PhaSePro: A comprehensive database of proteins driving liquid-liquid phase separation (LLPS) in living cells.
Additional web servers and databases we are involved in
Disordered Binding Site (DIBS) database is a repository for protein complexes that are formed between Intrinsically Disordered Proteins (IDPs) and globular/ordered partner proteins.
MobiDB: A database of protein disorder and mobility annotations
DisProt: A database of intrisically disordered proteins.