|
Zsuzsanna Dosztányi
Department of Biochemistry
|
Research interests
Understanding the structural and functional properties of intrinsically disordered proteins and their involvement in various diseases. Current research goals are: modeling the thermodynamic basis of order and disorder in proteins; recognizing functional sites within disordered proteins; understanding the specific roles of protein disorder in cancer. Various theoretical and computational approaches are utilized including simplified biophysical models, bioinformatic prediction methods and system biology approaches.
Selected publications
Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins. Nat Protoc. 2023 Nov;18(11):3157-3172.
Critical assessment of protein intrinsic disorder prediction. Nat Methods. 2021 May;18(5):472-481.
Mutations of Intrinsically Disordered Protein Regions Can Drive Cancer but Lack Therapeutic Strategies. Biomolecules. 2021 Mar 4;11(3):381.
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding. Nucleic Acids Res. 2018 Jul 2;46(W1):W329-W337.
Degrons in cancer. Sci Signal. 2017 Mar 14;10(470):eaak9982.
Complete publication list
Web servers
|
ANCHOR aims to predict binding regions in proteins that are disordered in isolation but can undergo a disorder-to-order transition upon binding to a structured protein partner. The approach is based on the energy estimation method and it uses a single amino acid sequence as an input. |
|
IUPred predicts intrinsically disoredered/unstructured proteins and protein regions. Intrinsically unstructured / disordered proteins have no single well-defined tertiary structure in their native, functional state. The IUPred server recognizes such regions from the amino acid sequence based on the estimated pairwise energy content. |