Together with Dr. János Réthelyi, Dr. Ágota Apáti and here research group (HUN-REN, TTK, EI), Our studies focus on the effect of some de novo mutation, previuosly associated with schisophrenia in various GWAS studies (KHSRP, LRRC7, KIR2DL1 and ZMYND11). In our patient derived induced pluripotent stem cells (iPSC) based neural stem cell lineages, we investigate the effect of individual pathogenic mutations on the cellular ROS level, the integrity of the mitochondrial network, the cells' ability to grow and survive, their differentiation capacity, and their elongation growth and gene expression characteristics.

SSB1 is closely related to the repair mechanism of a certain type of DNA damage associated with oxidative stress: the 8-oxoguanine formation. In connection with this known function, our research group led by Dr. Mihály Kovács showed that human SSB1 (due to its cysteine amino acid residues) is sensitive to various oxidative agents.

Currently I investigate changes in the subcellular localization of human SSB1 in the presence of various oxidizing agents in HELA, HEK and HFF1 cell lineages.

In the light of our results, the single-stranded DNA-binding proteins (SSB), belonge to an ancient and highli conserved protein family, contains several members (both bacterial and human orthologs) are able to form droplet-like separates (remaining in the liquid phase) by weak second-order interactions. Regarding their liquid-liquid phase separation (LLPS) propertiese we have both in vitro and in vivo results. In case of the human SSB1 protein, which so far has been recognised as an exclusively nuclear protein, we observed cytosolic enrichment under the influence of certain stressors. In the research group of Mihály Kovács we investigate the potential cytosolic function of this protein.