Matthias Müller, Dr. rer. nat.

Position: Akademischer Rat

Room no.: CP-02-109

Telephone no.: +49 (0)231 755 7066


Member of the group since: 03/2017

University Degree: Dr. rer. nat. in Biochemistry at the Max Planck Institute of Molecular Physiology


Earlier positions: PhD student and IMPRS fellow at the Max Planck Institute of Molecular Physiology (“Mechanismen der reversiblen enzymatischen Adenylylierung von Rab‐Proteinen”) under supervision of Prof. Dr. Roger S. Goody and Prof. Dr. Aymelt Itzen, Post-Doctoral fellow (with Prof. Dr. Roger S. Goody)

Diplom-Biochemiker, Martin-Luther-Universität Halle-Wittenberg

Expertise: X-Ray Crystallography, Biophysics

Off-Lab activities (hobbies): traveling, climbing



  1. Müller, M. P., Peters, H., Blumer, J., Blankenfeldt, W., Goody, R. S., and Itzen, A. (2010) The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b, Science 329, 946-949.
  2. Goody, R. S., Müller, M. P., Schoebel, S., Oesterlin, L. K., Blümer, J., Peters, H., Blankenfeldt, W., and Itzen, A. (2011) The versatile Legionella effector protein DrrA, Commun Integr Biol 4, 72-74.
  3. Smit, C., Blümer, J., Eerland, M. F., Albers, M. F., Müller, M. P., Goody, R. S., Itzen, A., and Hedberg, C. (2011) Efficient synthesis and applications of peptides containing adenylylated tyrosine residues, Angew Chem Int Ed Engl 50, 9200-9204.
  4. Goody, P. R., Heller, K., Oesterlin, L. K., Müller, M. P., Itzen, A., and Goody, R. S. (2012) Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins, EMBO J 31, 1774-1784.
  5. Müller, M. P., Shkumatov, A. V., Oesterlin, L. K., Schoebel, S., Goody, P. R., Goody, R. S., and Itzen, A. (2012) Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein, J Biol Chem 287, 35036-35046.
  6. Stein, M. P., Müller, M. P., and Wandinger-Ness, A. (2012) Bacterial pathogens commandeer Rab GTPases to establish intracellular niches, Traffic 13, 1565-1588.
  7. Müller, M. P., Albers, M. F., Itzen, A., and Hedberg, C. (2014) Exploring adenylylation and phosphocholination as post-translational modifications, Chembiochem 15, 19-26.
  8. Wiegandt, D., Vieweg, S., Hofmann, F., Koch, D., Li, F., Wu, Y. W., Itzen, A., Müller, M. P., and Goody, R. S. (2015) Locking GTPases covalently in their functional states, Nature communications 6, 7773.
  9. Koch, D., Rai, A., Ali, I., Bleimling, N., Friese, T., Brockmeyer, A., Janning, P., Goud, B., Itzen, A., Müller, M. P., and Goody, R. S. (2016) A pull-down procedure for the identification of unknown GEFs for small GTPases, Small GTPases 7, 93-106.
  10. Müller, M. P., and Goody, R. S. (2016) Review: Ras GTPases and myosin: Qualitative conservation and quantitative diversification in signal and energy transduction, Biopolymers 105, 422-430.
  11. Rai, A., Oprisko, A., Campos, J., Fu, Y., Friese, T., Itzen, A., Goody, R. S., Gazdag, E. M., and Müller, M. P. (2016) bMERB domains are bivalent Rab8 family effectors evolved by gene duplication, Elife 5.
  12. Goody, R. S., Müller, M. P., and Wu, Y. W. (2017) Mechanisms of action of Rab proteins, key regulators of intracellular vesicular transport, Biol Chem 398, 565-575.
  13. Müller, M. P., and Goody, R. S. (2017) Molecular control of Rab activity by GEFs, GAPs and GDI, Small GTPases, 1-17.
  14. Rai, A., Goody, R. S., and Müller, M. P. (2017) Multivalency in Rab effector interactions, Small GTPases, 1-7.
  15. Müller, M. P., Jeganathan, S., Heidrich, A., Campos, J., and Goody, R. S. (2017) Nucleotide based covalent inhibitors of KRas can only be efficient in vivo if they bind reversibly with GTP-like affinity, Sci Rep 7, 3687.
  16. Bührmann, M., Wiedemann, B. M., Müller, M. P., Hardick, J., Ecke, M., and Rauh, D. (2017) Structure-based design, synthesis and crystallization of 2-arylquinazolines as lipid pocket ligands of p38alpha MAPK, Plos One 12, e0184627.
  17. Cigler, M., Müller, T. G., Horn-Ghetko, D., von Wrisberg, M. K., Fottner, M., Goody, R. S., Itzen, A., Müller, M. P., and Lang, K. (2017) Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo, Angew Chem Int Ed Engl 56, 15737-15741.
  18. Müller, M. P., and Rauh, D. (2018) Try Me: Promiscuous Inhibitors Still Allow for Selective Targeted Protein Degradation, Cell Chem Biol 25, 4-6.
  19. Wolle, P., Müller, M. P., and Rauh, D. (2018) Augmented Reality in Scientific Publications-Taking the Visualization of 3D Structures to the Next Level, ACS chemical biology 13, 496-499.
  20. Ali, I., Eu, S., Koch, D., Bleimling, N., Goody, R. S., and Müller, M. P. (2018) Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae, Acta Crystallographica Section F 74.
  21. Jeganathan, S., Müller, M. P., Imtiaz, A., and Goody, R. S. (2018) Assays for nucleotide-competitive reversible and irreversible inhibitors of Ras GTPases, Biochemistry.
  22. Tesch, R., Becker, C., Müller, M. P., Beck, M. E., Quambusch, L., Getlik, M., Lategahn, J., Uhlenbrock, N., Costa, F. N., Polêto, M. D., de Sena Murteira Pinheiro, P., Rodrigues, D. A., Sant'Anna, C. M., Ferreira, F. F., Verli, H., Fraga, C. A. M., and Rauh, D. (2018) An Unusual Intramolecular Halogen Bond guides Conformational Selection, Angew Chem Int Ed Engl.