University of Dundee


The School of Research of The College of Life Sciences, University of Dundee, directed by Mike Ferguson, is housed in modern, state of the art research buildings and is one of the leading such centres in Europe. Ferguson is a fellow of The Royal Society, a member of EMBO and has won several prizes. He is well known for his pioneering work on glycosylphosphatidylinositol (GPI) membrane anchor structure/biosynthesis and parasite glycobiology. He has published over 260 peer-reviewed and runs a research group of 12 people. He is also Director of an advanced Proteomics facility. Ferguson is also a founding member of the Drug Discovery Unit (DDU - see, a fully integrated unit with medicinal and computational chemistry, structural biology and DMPK facilities to translate basic science into therapeutic agents.

The College of Life has superb core facilities for X-ray crystallography, NMR, FACS, high-performance computing, electron microscopy, light microscopy, analytical ultracentrifugation, isothermal titration calorimetry, light scattering, Biacore surface plasmon resonance and a sophisticated Proteomics facility with 4 Thermo Orbitrap Velos, 2 Orbitrap XL, 1 Agilent 6520 Q-Tof and 2 ABI Q-Trap 4000 LC-MS/MS systems. Dedicated containment facility for growth and genetic manipulation of protozoan parasites.


1) Ferguson, M.A.J., Homans, S.W., Dwek, R.A. and Rademacher, T.W. (1988) Glycosylphosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane. Science 239, 753-759.
2) Roper, J.R., Güther, M.L.S., Milne, K.G. and Ferguson, M.A.J. (2002) Galactose metabolism is essential for the African sleeping sickness parasite Trypanosoma brucei. Proc. Natl. Acad. Sci. (USA) 99, 5884-5889.
3) Stokes, M.J., Güther, M.L.S., Turnock, D.C., Martin, K.L., Alphey, M.S. and Ferguson, M.A.J. (2008) The synthesis of UDP-N-acetylglucosamine is essential for bloodstream form Trypanosoma brucei in vitro and in vivo and UDP-N-acetylglucosamine starvation reveals a hierarchy in parasite protein glycosylation. J. Biol. Chem. 283, 16147-16161.