RESEARCH SUMMARY
Currently, our research focused on the identification of protein-protein interactions by quantitative Förster resonance energy transfer (FRET) measurements as well as by fluorescence intensity ratio (FIR) analysis in live cells. We are interested in G-protein Coupled Receptor (GPCR) dimerization and the effects of post-translational modifications and ligand interactions on receptor dimerization.
Research Interest: Membrane proteins, Protein-protein interactions, GPCRs, nAChRs, Fluorescence proteins, Confocal microscopy, Total Internal Reflection Fluorescence microscopy, FRET, HPLC, Mass spectrometry, MALDI-TOF, protein purification, Photo affinity cross-linking
SELECTED PUBLICATIONS
Cevheroğlu, O., Murat, M., Mingu-Akmete, S., & Son, Ç. D. (2021). Ste2p Under the Microscope: the Investigation of Oligomeric States of a Yeast G Protein-Coupled Receptor. The journal of physical chemistry. B, 125(33), 9526–9536. doi: 10.1021/acs.jpcb.1c05872
Aydın, A. D., Altınel, F., Erdoğmuş, H., & Son, Ç. D. (2021). Allergen fragrance molecules: a potential relief for COVID-19. BMC complementary medicine and therapies, 21(1), 41. doi: 10.1186/s12906-021-03214-4
Cevheroğlu, O., Becker, J. M., & Son, Ç. D. (2017). GPCR-Gα protein precoupling: Interaction between Ste2p, a yeast GPCR, and Gpa1p, its Gα protein, is formed before ligand binding via the Ste2p C-terminal domain and the Gpa1p N-terminal domain. Biochimica et biophysica acta. Biomembranes, 1859(12), 2435–2446. doi: 10.1016/j.bbamem.2017.09.022
Cevheroğlu, O., Kumaş, G., Hauser, M., Becker, J. M., & Son, Ç. D. (2017). The yeast Ste2p G protein-coupled receptor dimerizes on the cell plasma membrane. Biochimica et biophysica acta. Biomembranes, 1859(5), 698–711. doi: 10.1016/j.bbamem.2017.01.008
Son, C. D., Moss, F. J., Cohen, B. N., & Lester, H. A. (2009). Nicotine normalizes intracellular subunit stoichiometry of nicotinic receptors carrying mutations linked to autosomal dominant nocturnal frontal lobe epilepsy. Molecular pharmacology, 75(5), 1137–1148. doi: 10.1124/mol.108.054494
