Team
Team

Matthias Müller, Dr. rer. nat.

Position: Academic Council

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

 

Publications:

  1. Goebel, L.; Müller, M. P.; Goody, R. S.; Rauh, D.. KRasG12C inhibitors in clinical trials: a short historical perspective. RSC Med. Chem. 2020, 11 (7), 760–770.

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  2. Lategahn, J.; Hardick, J.; Grabe, T.; Niggenaber, J.; Jeyakumar, K.; Keul, M.; Tumbrink, H. L.; Becker, C.; Hodson, L.; Kirschner, T.; Klövekorn, P.; Ketzer, J.; Baumann, M.; Terheyden, S.; Unger, A.; Weisner, J.; Müller, M. P.; van Otterlo, W. A. L.; Bauer, S.; Rauh, D.. Targeting Her2-insYVMA with Covalent Inhibitors-A Focused Compound Screening and Structure-Based Design Approach. J. Med. Chem. 2020, 63 (20), 11725–11755.

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  3. Baumann, M.; Depta, L.; Dienstbier, N.; Gontla, R.; Günther, G.; Hahn, S. A.; Hardick, J.; Hengstler, J. G.; Ladigan, S.; Landel, I.; Lindemann, M.; Maghnouj, A.; Müller, H.; Müller, M. P.; Pohl, M.; Quambusch, L.; Rauh, D.; Reintjes, C.; Scheinpflug, R.; Schultz-Fademrecht, C.; Siveke, J. T.; Smith, S.; Tannapfel, A.; Teschendorf, C.; Trajkovic-Arsic, M.; Uhl, W.; Uhlenbrock, N.; Unger, A.; Viebahn, R.; Weisner, J.; Wolters, H.. Preclinical Efficacy of Covalent-Allosteric AKT Inhibitor Borussertib in Combination with Trametinib in KRAS-Mutant Pancreatic and Colorectal Cancer. Cancer Res. 2019, 79 (9), 2367–2378.

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  4. Goody, R. S.; Müller, M. P.; Rauh, D.. Mutant-Specific Targeting of Ras G12C Activity by Covalently Reacting Small Molecules. Cell Chem. Biol. 2019, 26 (10), 1338–1348.

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  5. Lategahn, J.; Keul, M.; Klövekorn, P.; Tumbrink, H. L.; Niggenaber, J.; Müller, M. P.; Hodson, L.; Flaßhoff, M.; Hardick, J.; Grabe, T.; Engel, J.; Schultz-Fademrecht, C.; Baumann, M.; Ketzer, J.; Mühlenberg, T.; Hiller, W.; Günther, G.; Unger, A.; Müller, H.; Heimsoeth, A.; Golz, C.; Blank-Landeshammer, B.; Kollipara, L.; Zahedi, R. P.; Strohmann, C.; Hengstler, J. G.; van Otterlo, W. A. L.; Bauer, S.; Rauh, D.. Inhibition of osimertinib-resistant epidermal growth factor receptor EGFR-T790M/C797S. Chem. Sci. 2019, 10 (46), 10789–10801.

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  6. a) Quambusch, L.; Landel, I.; Depta, L.; Weisner, J.; Uhlenbrock, N.; Müller, M. P.; Glanemann, F.; Althoff, K.; Siveke, J. T.; Rauh, D.. Covalent-Allosteric Inhibitors to Achieve Akt Isoform-Selectivity. Angew. Chem. Int. Ed Engl. 2019, 58 (52), 18823–18829.

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    b) Quambusch, L.; Landel, I.; Depta, L.; Weisner, J.; Uhlenbrock, N.; Müller, M. P.; Glanemann, F.; Althoff, K.; Siveke, J. T.; Rauh, D.. Covalent‐Allosteric Inhibitors to Achieve Akt Isoform‐Selectivity. Angew. Chem. 2019, 131 (52), 18999–19005.

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  7. Rai, A.; Goody, R. S.; Müller, M. P.. Multivalency in Rab effector interactions. Small GTPases 2019, 10 (1), 40–46.

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  8. Schehr, M.; Ianes, C.; Weisner, J.; Heintze, L.; Müller, M. P.; Pichlo, C.; Charl, J.; Brunstein, E.; Ewert, J.; Lehr, M.; Baumann, U.; Rauh, D.; Knippschild, U.; Peifer, C.; Herges, R.. 2-Azo-, 2-diazocine-thiazols and 2-azo-imidazoles as photoswitchable kinase inhibitors: limitations and pitfalls of the photoswitchable inhibitor approach. Photochem. Photobiol. Sci. 2019, 18 (6), 1398–1407.

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  9. Uhlenbrock, N.; Smith, S.; Weisner, J.; Landel, I.; Lindemann, M.; Le, T. A.; Hardick, J.; Gontla, R.; Scheinpflug, R.; Czodrowski, P.; Janning, P.; Depta, L.; Quambusch, L.; Müller, M. P.; Engels, B.; Rauh, D.. Structural and chemical insights into the covalent-allosteric inhibition of the protein kinase Akt. Chem. Sci. 2019, 10 (12), 3573–3585.

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  10. Ali, I.; Eu, S.; Koch, D.; Bleimling, N.; Goody, R. S.; Müller, M. P.. Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae. Acta Crystallogr. F 2018, 74 (Pt 5), 315–321.

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  11. Jeganathan, S.; Müller, M. P.; Ali, I.; Goody, R. S.. Assays for Nucleotide Competitive Reversible and Irreversible Inhibitors of Ras GTPases. Biochemistry 2018, 57 (31), 4690–4699.

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  12. Müller, M. P.; Goody, R. S.. Molecular control of Rab activity by GEFs, GAPs and GDI. Small GTPases 2018, 9 (1-2), 5–21.

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  13. Müller, M. P.; Rauh, D.. Try Me: Promiscuous Inhibitors Still Allow for Selective Targeted Protein Degradation. Cell Chem. Biol. 2018, 25 (1), 4–6.

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  14. a) Tesch, R.; Becker, C.; Müller, M. P.; Beck, M. E.; Quambusch, L.; Getlik, M.; Lategahn, J.; Uhlenbrock, N.; Costa, F. N.; Polêto, M. D.; Pinheiro, P. d. S. M.; Rodrigues, D. A.; Sant'Anna, C. M. R.; Ferreira, F. F.; Verli, H.; Fraga, C. A. M.; Rauh, D.. An Unusual Intramolecular Halogen Bond Guides Conformational Selection. Angew. Chem. Int. Ed Engl. 2018, 57 (31), 9970–9975.

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    b) Tesch, R.; Becker, C.; Müller, M. P.; Beck, M. E.; Quambusch, L.; Getlik, M.; Lategahn, J.; Uhlenbrock, N.; Costa, F. N.; Polêto, M. D.; Pinheiro, P. d. S. M.; Rodrigues, D. A.; Sant'Anna, C. M. R.; Ferreira, F. F.; Verli, H.; Fraga, C. A. M.; Rauh, D.. Eine ungewöhnliche intramolekulare Halogenbindung führt zu konformationeller Selektion. Angew. Chem. 2018, 130 (31), 10120–10126.

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  15. Wolle, P.; Müller, M. P.; Rauh, D.. Augmented Reality in Scientific Publications-Taking the Visualization of 3D Structures to the Next Level. ACS Chem. Biol. 2018, 13 (3), 496–499.

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  16. Bührmann, M.; Wiedemann, B. M.; Müller, M. P.; Hardick, J.; Ecke, M.; Rauh, D.. Structure-based design, synthesis and crystallization of 2-arylquinazolines as lipid pocket ligands of p38α MAPK. PloS one 2017, 12 (9), e0184627.

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  17. a) Cigler, M.; Müller, T. G.; Horn-Ghetko, D.; Wrisberg, M.-K. von; Fottner, M.; Goody, R. S.; Itzen, A.; Müller, M. P.; Lang, K.. Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo. Angew. Chem. Int. Ed Engl. 2017, 56 (49), 15737–15741.

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    b) Cigler, M.; Müller, T. G.; Horn-Ghetko, D.; Wrisberg, M.-K. von; Fottner, M.; Goody, R. S.; Itzen, A.; Müller, M. P.; Lang, K.. Proximitäts-vermittelte kovalente Stabilisierung niedrig-affiner Proteinkomplexe in vitro und in vivo. Angew. Chem. 2017, 129 (49), 15943–15947.

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  18. Goody, R. S.; Müller, M. P.; Wu, Y.-W.. Mechanisms of action of Rab proteins, key regulators of intracellular vesicular transport. Biol. Chem. 2017, 398 (5-6), 565–575.

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  19. Koch, D.; Rai, A.; Ali, I.; Bleimling, N.; Friese, T.; Brockmeyer, A.; Janning, P.; Goud, B.; Itzen, A.; Müller, M. P.; Goody, R. S.. A pull-down procedure for the identification of unknown GEFs for small GTPases. Small GTPases 2016, 7 (2), 93–106.

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  20. Mueller, M. P.; Goody, R. S.. Review: Ras GTPases and myosin: Qualitative conservation and quantitative diversification in signal and energy transduction. Biopolymers 2016, 105 (8), 422–430.

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  21. Rai, A.; Oprisko, A.; Campos, J.; Fu, Y.; Friese, T.; Itzen, A.; Goody, R. S.; Gazdag, E. M.; Müller, M. P.. bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. eLife 2016, 5.

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  22. Wiegandt, D.; Vieweg, S.; Hofmann, F.; Koch, D.; Li, F.; Wu, Y.-W.; Itzen, A.; Müller, M. P.; Goody, R. S.. Locking GTPases covalently in their functional states. Nat. Commun. 2015, 6, 7773.

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  23. Müller, M. P.; Albers, M. F.; Itzen, A.; Hedberg, C.. Exploring adenylylation and phosphocholination as post-translational modifications. ChemBioChem 2014, 15 (1), 19–26.

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  24. Goody, P. R.; Heller, K.; Oesterlin, L. K.; Müller, M. P.; Itzen, A.; Goody, R. S.. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J. 2012, 31 (7), 1774–1784.

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  25. Müller, M. P.; Shkumatov, A. V.; Oesterlin, L. K.; Schoebel, S.; Goody, P. R.; Goody, R. S.; Itzen, A.. Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein. J. Biol. Chem. 2012, 287 (42), 35036–35046.

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  26. Stein, M.-P.; Müller, M. P.; Wandinger-Ness, A.. Bacterial pathogens commandeer Rab GTPases to establish intracellular niches. Traffic 2012, 13 (12), 1565–1588.

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  27. Goody, R. S.; Müller, M. P.; Schoebel, S.; Oesterlin, L. K.; Blümer, J.; Peters, H.; Blankenfeldt, W.; Itzen, A.. The versatile Legionella effector protein DrrA. Commun. Integr. Biol. 2011, 4 (1), 72–74.

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  28. a) Smit, C.; Blümer, J.; Eerland, M. F.; Albers, M. F.; Müller, M. P.; Goody, R. S.; Itzen, A.; Hedberg, C.. Efficient synthesis and applications of peptides containing adenylylated tyrosine residues. Angew. Chem. Int. Ed Engl. 2011, 50 (39), 9200–9204.

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    b) Smit, C.; Blümer, J.; Eerland, M. F.; Albers, M. F.; Müller, M. P.; Goody, R. S.; Itzen, A.; Hedberg, C.. Effiziente Synthese und Anwendung von Peptiden mit adenylylierten Tyrosinresten. Angew. Chem. 2011, 123 (39), 9367–9371.

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  29. Müller, M. P.; Peters, H.; Blümer, J.; Blankenfeldt, W.; Goody, R. S.; Itzen, A.. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 2010, 329 (5994), 946–949.

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