Our department develops and applies methods of mass spectrometry (MS)-based proteomics in a variety of biological areas. Most of these projects are performed within the department but some are also done in long-term collaboration with other groups. In the last two years we have published more than 50 papers and we are one of the most highly cited research groups in Europe and world-wide according to the Institute for Scientific Information.
Highlights during the last two years have been the development of methods in proteomic sample preparation (Wisniewski et al. Nature Methods 2009) and in computational proteomics, in particular the MaxQuant family of algorithms, which are now widely used (Cox and Mann, Nature Biotechnology, 2008).
These developments have led to the first identification and quantification of a model system proteome, of the yeast model system (de Godoy et al. Nature 2008).
As we have argued recently, these developments now put proteomics on an equal footing with other genomics and post-genomics technologies (Cox and Mann, Cell, 2007). Unlike genomics technologies, however, proteomics can directly and quantitatively determine the modification state of proteins.
During the last few years, we have described a plethora of phosphorylation sites (Olsen et al. Cell, 2006), lysine acetylation sites (Choudhary et al. Science 2009) and glycosylation sites (Zielinska et al. Cell 2010) in the human proteome.