General Support for Biological Research:
We continuously supported biological research at the EMBL and outside according to our capacity.
Examples: 

    •    quantitative profiling of sarcomere associated proteins in limp and extraocular muscle (slide 10) [1, 2]

    •    studying the splicing mechanism by protein complex purification and sequencing at different stages of the splicing process [3]

    •    Nup155’s role in nuclear envelope and nuclear pore formation [4]

Proteomics Visitor Laboratory:

In 2001 we spent a considerable amount of time to establish the proteomics visitor laboratory sponsored by Waters and Biorad (slide 1-9). This visitor laboratory evolved into EMBL’s proteomics core facility. 

Spin-Off Companies:

Two spin-off companies are directly related to main projects of our group, Protana, which later split off Proxeon, and CellZome.

References

• Fraterman, S., U. Zeiger, T.S. Khurana, M. Wilm, and N.A. Rubinstein, Quantitative proteomic profiling of sarcomere associated proteins in limb and extraocular muscle allotypes. Mol Cell Proteomics, 2007.

• • Fraterman, S., U. Zeiger, T.S. Khurana, N.A. Rubinstein, and M. Wilm, Combination of peptide OFFGEL fractionation and label-free quantitation facilitated proteomics profiling of extraocular muscle. Proteomics, 2007. 7(18): p. 3404-16.
• • Makarova, O.V., E.M. Makarov, H. Urlaub, C.L. Will, M. Gentzel, M. Wilm, and R. Luhrmann, A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing. Embo J, 2004. 23(12): p. 2381-91.
• • Franz, C., P. Askjaer, W. Antonin, C.L. Iglesias, U. Haselmann, M. Schelder, A. de Marco, M. Wilm, C. Antony, and I.W. Mattaj, Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates. Embo J, 2005. 24(20): p. 3519-31.