Short CV/Education and training

  • 1977
    General Teacher Certificate – Ministry of Education, Singapore

  • 1981
    BSc. Joint Honors in Biology & Chemistry – University of Stirling, Scotland, UK

  • 1984
    PhD in Chemistry – University of Stirling, Scotland, UK

  • 1984 – 1986
    Post-doc, Department of Biochemistry, Oxford University, UK

  • 1986 – 1987
    Post-doc, Louis Pasteur Institute, Strasbourg, FR

  • 1987 – 1989
    Post-doc, Institute für Physikalische Biochemie, Munich, DE

  • 1989 – 1990
    Post-doc, Jules Stein Eye Institute, Los Angeles, USA

  • 1991 – 1996
    Research Associate, Department of Cellular Biochemistry and Biophysics, Sloan-Kettering Institute, New York, USA

  • 1997 – 2005
    Research Group Leader, Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, DE

  • Since 2006
    Independent Research Group Leader and Principal Investigator, Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, DE

Selected publications

  • Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475(7356), 324-332.

  • Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature 479(7372), 194-199.

  • Stotz, M., Mueller-Cajar, O., Ciniawsky, S., Wendler, P., Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Structure of green-type Rubisco activase from tobacco. Nat. Struct. Mol. Biol. 18(12), 1366-1370.

  • Georgescauld, F., Popova, K., Gupta, A.J., Bracher, A., Engen, J.R., Hayer-Hartl, M. and Hartl, F.U. (2014). GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding. Cell 157(4), 922-934.

  • Bracher, B., Sharma, A., Starling-Windhof, A., Hartl, F.U. and Hayer-Hartl, M. (2015). Degradation of potent Rubisco inhibitor by selective sugar phosphatase. Nat. Plants 1, Article# 14002 (doi: 10.1038/nplants.2014.2).

  • Durao, P., Aigner, H., Nagy, P., Muellar-Cajar, O., Hartl, F.U. and Hayer-Hartl, M. (2015). Opposing effects of folding and assembly chaperones on evolvability of Rubisco. Nat. Chem. Biol. 11(2), 148-155.

  • Hauser, T., Popilka, L., Hartl, F.U. and Hayer-Hartl, M. (2015). Role of auxiliary proteins in Rubisco biogenesis and function. Nat. Plants 1, Article# 15065 (doi: 10.1038/nplants.2015.65).

  • Hauser, T., Bhat, J., Miličić, G., Wendler, P., Hartl, F.U., Bracher, B. and Hayer-Hartl, M. (2015). Structure and mechanism of the Rubisco assembly chaperone Raf1. Nat. Struct. Mol. Biol. 22(9), 720-728. (doi: 10.1038/nsmb.3062).

  • Hayer-Hartl, M., Bracher, B. and Hartl, F.U. (2016). The GroEL-GroES chaperonin machine – a nano-cage for protein folding. Trends Biochem. Sci. 41(1), 62-76. doi: 10.1016/j.tibs.2015.07.009).

  • Balchin, D., Hayer-Hartl, M. and Hartl, F.U. (2016). In vivo aspects of protein folding and quality control. Science 353(6294), aac4354 (doi: 10.1126/science.aac4354).


Membership in scientific bodies/juries

  • Member of Editorial Board, eLIFE

  • Member of the European Molecular Biology Organization (EMBO)

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