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.
Our group is involved in EU funded projects IDPro and IDPFun2. We are coordinating the Twinning grant starting in October 1st, 2024 with partners Prof. Michele Vendruscolo (University of Cambridge), Prof. Markus Zweckstetter (German Center for Neurodegenerative Diseases), Pro. Silvio Tossato (University of Padova).
Selected publications
- AIUPred: combining energy estimation with deep learning for the enhanced prediction of protein disorder
Gábor Erdős, Zsuzsanna Dosztányi
Nucleic Acids Research, Volume 52, Issue W1, 5 July 2024, Pages W176–W181, https://doi.org/10.1093/nar/gkae385 - 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
Services
 | AIUPred: Prediction of Intrinsically Unstructured Proteins |
 | DisCanVis: Integrating structural and functional annotations for the better understanding of the effect of cancer mutations located within disordered proteins. |
 | 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 |
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 | 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. |
Funding
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