Professor Clemens Kaminski
Professor Clemens Kaminski is pleased to consider applications from prospective PhD students.
Using microscopic techniques such as Fluorescent Resonance Energy Transfer (FRET), Fluorescence Lifetime Imaging Microscopy (FLIM) and dynamic imaging we can study chemistry and molecular transport directly within the living cell. A major effort is invested in the development of techniques for the study of protein-protein interactions, which are linked to disease, in particular to cancer, Parkinson's disease and Malaria. The techniques are also used for research into molecular assembly, protein conformational dynamics, and aggregation. Recently we have developed an optical superresolution microscope based on dSTORM (direct Stochastic Optical Reconstruction Microscopy) with which we can perform structural or colocalisation microscopies at molecular scale resolution.
FLIM TCSPC FRET FRAP Superresolution imaging
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Kaminski Schierle GS, van de Linde S, Erdelyi M, Esbjörner EK, Klein T, Rees E, Bertoncini CW, Dobson CM, Sauer M, and Kaminski CF (2011), In Situ Measurements of the Formation and Morphology of Intracellular ß-Amyloid Fibrils by Super-Resolution Fluorescence Imaging, J. Am. Chem. Soc., 133 (33), pp 12902?12905 Kaminski Schierle GS, Bertoncini CW, Chan FTS, van der Goot AT, Schwedler S, Skepper J, Schlachter S, van Ham T, Esposito A, Kumita JR, Nollen EAA, Dobson CM, Kaminski CF (2011), A FRET sensor for non-invasive imaging of amyloid formation in vivo, ChemPhysChem, 12(3), 673?680, Elder AD, Domin A, Kaminski Schierle GS, Lindon C, Pines J, Esposito A, and Kaminski CF (2009), A quantitative protocol for dynamic measurements of protein interactions by FRET-sensitized fluorescence emission. Journal of the Royal Society Interface, Volume 6, S59-S81.