Dr. Manajit Hayer-Hartl

• 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
  
  

• 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).

• Member of Editorial Board, eLIFE

• Member of the European Molecular Biology Organization (EMBO)

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