My interest for research began during my bachelor in Physical education (1984-1988) at the Catholic University in Belgium thanks to Professor G. Maréchal my Physiology teacher. This initial interest further developed during my MSc (1990) and PhD (1993) when I investigated the function of Dystrophin in a murine model of the Duchenne Muscular Dystrophy. My PhD was followed by a first postdoctoral position in Professor Cris dos Remedios laboratory at the University of Sydney. Cris introduced me to the wonderful world of fluorescence spectroscopy. In 1998, I returned to Europe for two years at the University of Bordeaux in France. This period in Europe gave me the opportunity to learn molecular biology techniques. I then joined the laboratory of Prof. David M Jameson in Hawaii in 2000. In his laboratory, I established a molecular biology section and broadened and deepened my knowledge on the application of fluorescence to biological systems. I arrived at the University of New England in April of 2003 where I started my academic career.
I have a continued interest in understanding the molecular basis and the dynamics of protein interaction.
My current research focuses on the motility of non-muscle cells. Particularly in the signaling pathway linking the membrane receptors to the cytoskeleton and the role of this pathway in human cancer.
P.D.J. Moens and L.A. Bagatolli, Profilin binding to sub-micellar concentrations of phosphatidylinositol (4,5) bisphosphate and phosphatidylinositol (3,4,5) trisphosphate, Biochimica Biophysica Acta, vol. 1768, pp. 439-449, 2007.
Moens P. D. J., Wahl M. C. and Jameson D. M., Oligomeric State and Mode of Self-Association of Thermotoga maritima Ribosomal Stalk Protein L12 in Solution, Biochemistry, vol. 44, pp. 3298-3305, 2005.
Jameson D. M., Croney J. C. and Moens P. D., J. Fluorescence: basic concepts, practical aspects, and some anecdotes, Methods Enzymol, vol. 360, pp. 1-43, 2003.
Moens P. D. and dos Remedios C. G., A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374, Biochemistry, vol. 36, pp. 7353-7360, 1997.
M. Kekic, W. Huang, P.D. Moens, B.D. Hambly and C.G. dos Remedios, Distance measurements near the myosin head-rod junction using fluorescence spectroscopy, Biophys J, vol. 71, pp. 40-47, 1996.
Moens P. D., Van-Schoor M. C. and Marechal G., Lack of myoblasts migration between transplanted and host muscles of mdx and normal mice, J Muscle Res Cell Motil, vol. 17, pp. 37-43, 1996.
dos Remedios C. G. and Moens P. D., Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor, J Struct Biol, vol. 115, pp. 175-185, 1995.
dos Remedios C. G. and Moens P. D., Actin and the actomyosin interface: a review, Biochim Biophys Acta, vol. 1228, pp. 99-124, 1995.
Moens P. D., Yee D. J. and dos Remedios C. G., Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assembly, Biochemistry, vol. 33, pp. 13102-13108, 1994.
Moens P., Baatsen P. H. and Marechal G., Increased susceptibility of EDL muscles from mdx mice to damage induced by contractions with stretch, J Muscle Res Cell Motil, vol. 14, pp. 446-451, 1993.