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

  • PhaSePro: the database of proteins driving liquid–liquid phase separation
    Bálint Mészáros, Gábor Erdős, Beáta Szabó, Éva Schád, Ágnes Tantos, Rawan Abukhairan, Tamás Horváth, Nikoletta Murvai, Orsolya P Kovács, Márton Kovács, Silvio C E Tosatto, Péter Tompa, Zsuzsanna Dosztányi, Rita Pancsa
    Nucleic Acids Research, October 2019, https://doi.org/10.1093/nar/gkz848
  • IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding
    Bálint Mészáros, Gábor Erdős, Zsuzsanna Dosztányi
    Nucleic Acids Research, July 2018, https://doi.org/10.1093/nar/gky384
  • Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway
    Gábor Erdős, Tamás Szaniszló, Mátyás Pajkos, Borbála Hajdu-Soltész, Bence Kiss, Gábor Pál, László Nyitray, Zsuzsanna Dosztányi
    PLOS Compl. Biol., November 2017, https://doi.org/10.1371/journal.pcbi.1005885
  • Degrons in cancer
    Bálint Mészáros, Manjeet Kumar, Toby J. Gibson, Bora Uyar, Zsuzsanna Dosztányi
    Cell Signaling, March 2017, https://doi.org/10.1126/scisignal.aak9982
  • Large-Scale Analysis of Redox-Sensitive Conditionally Disordered Protein Regions Reveals Their Widespread Nature and Key Roles in High-Level Eukaryotic Processes
    Gábor Erdős, Bálint Mészáros, Dana Reichmann, Zsuzsanna Dosztányi
    Proteomics, January 2019, https://doi.org/10.1002/pmic.201800070


IUPred3: Prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation
MemMoRF is a comprehensive database of transmembrane and membrane associated proteins with MemMoRFs: regions that undergo disorder-to-order transition or large conformational changes upon membrane association.
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.