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Dr Franz-Ulrich Hartl, Known For His Pioneering Work In The Field Of Protein-Mediated Protein Folding PDF Print E-mail
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Monday, 03 May 2010 00:56

Franz-Ulrich Hartl (born March 10, 1957) is a German biochemist and Managing Director of the Max Planck Institute of Biochemistry. He is known for his pioneering work in the field of protein-mediated protein folding.

F. Ulrich Hartl studied Medicine at Heidelberg University. After receiving his M.D. in 1982 and his doctoral degree in Biochemistry in 1985 he moved to the laboratory of Walter Neupert in Munich where he worked on the mechanism of protein transport into mitochondria, first as a post-doctoral fellow and from 1987 to 1991 as a research group leader.

In 1988 he initiated the work on molecular chaperones and demonstrated, collaboratively with A. Horwich, the basic role of chaperones in assisting protein folding. The period in Walter Neupert’s department was interrupted by a stay in William Wickner’s laboratory at UCLA (1989/1990), where Hartl worked on the mechanism of bacterial protein export. After returning to Munich he received his Habilitation in Biochemistry and soon after accepted an offer from Sloan-Kettering Cancer Center in New York to join the newly-founded department of James Rothman as an Associate Member.

Between 1991 and 1997 he investigated the mechanisms of protein folding in the bacterial and eukaryotic cytosol. He reconstituted the pathway of chaperone-assisted folding in which the Hsp70 and the GroEL chaperone systems cooperate and discovered that GroEL and its co-factor GroES provide a nano-cage for single protein molecules to fold unimpaired by aggregation. In 1993 Hartl was promoted to Member with tenure, and in 1994 became an Investigator of the Howard Hughes Medical Institute. In 1997 he returned to Munich to head the Department of Cellular Biochemistry at the Max Planck Institute of Biochemistry (MPIB). At MPIB Ulrich Hartl continues to investigate the mechanisms of cellular protein folding using a range of methods from cell biology, biochemistry and structural biology. In addition, he initiated research into neurodegenerative diseases caused by protein misfolding and aggregation. This work led to the finding that chaperones can effectively inhibit the formation of amyloid aggregates associated with neurodegeneration. Much of this work was done in collaboration with Manajit Hayer-Hartl.

Hartl received the following honours:

1999 Academy Award of the Berlin-Brandenburg Academy of Sciences and Humanities
2004 Gairdner Foundation International Award jointly with Arthur L. Horwich
2005 Ernst Jung-Prize for Medicine
2006 Stein and Moore Award of the Protein Society
2006 Koerber European Science Award
2007 Wiley Prize in Biomedical Science jointly with Arthur L. Horwich of Yale School of Medicine, "for their significant contribution in protein folding".[1]
2008 Lewis S. Rosenstiel Award for Distinguished Work in Basic Medical Science jointly with Arthur L. Horwich "for their pioneering work in the field of protein-mediated protein folding"[2]
2008 Louisa Gross Horwitz Prize for Biology or Biochemistry jointly with Arthur L. Horwich

 
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