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Matthias Hentze (born 25 January 1960 in Wiedenbrück, now Rheda-Wiedenbrück, Germany is a German scientist and medical doctor.

Biography
Matthias Hentze obtained his Abitur from the Ratsgymnasium in Rheda-Wiedenbrück in 1978. He studied medicine at the Westfälische Wilhelms-Universität in Münster (Germany) as well as the Medical Schools of Southampton, Oxford, Glasgow and Cambridge (U.K.). In 1984 he obtained the German medical board certification (‘Approbation als Arzt’) and received his doctoral degree (M.D.) from the University of Münster for his work on lysosomal enzyme biogenesis and transport in the laboratory of Prof. Kurt von Figura. In 1990, he obtained his ‘Habilitation’ at the University of Heidelberg (Germany).

Matthias Hentze is married to the German medical doctor Sabine Hentze and has three daughters. He regularly participates in city marathons of the World Marathon Majors series (New York, Boston, Chicago, London, Berlin).

Professional career
After a brief residency in internal medicine, Matthias Hentze joined the laboratory of Richard D. Klausner at the National Institutes of Health (Bethesda, Maryland, USA) as a postdoctoral fellow supported by a fellowship from the Deutsche Forschungsgemeinschaft in 1985. In 1987, Hentze and his colleagues discovered iron-responsive elements (IRE), showing for the first time gene regulation at the translational level in animal cells. In 1989, he joined the European Molecular Biology Laboratory in Heidelberg as a group leader. In 1996, he was appointed as “Dean” of the EMBL International PhD Programme, a position that he held until 2005 when he became “Associate Director” of the EMBL. In the same year, he became Professor for Molecular Medicine at the University of Heidelberg. Together with Prof. Andreas Kulozik of the Medical Faculty of Heidelberg University, Hentze co-founded the ‘Molecular Medicine Partnership Unit (MMPU)’ (2002) and serves as its Co-Director. As the first institutional partnership between the EMBL and a national institution, the MMPU pioneers interdisciplinary research at the interface between molecular biology and clinical medicine. Hentze’s research team has pioneered the field of translational control by regulatory factors (RNA-binding proteins, microRNAs), which is now recognized to play important roles in development, central nervous system function, cancer and many other diseases. Hentze is also credited for key discoveries in the field of the molecular control of iron metabolism and its diseases. Within the MMPU, he contributes to investigations into diseases of RNA metabolism, especially on nonsense-mediated decay (NMD) and 3’end formation.

Hentze is a co-founder of Anadys Pharmaceuticals (San Diego).

Honors, awards and society memberships
Hentze is an elected member of the German National Academy of Sciences Leopoldina, the European Academy of Sciences, and the European Molecular Biology Organization (EMBO). His most valuable awards include the Gottfried Wilhelm Leibniz Prize, Germany’s highest research honor (2000) and the Lautenschlaeger Research Prize of Heidelberg University in 2007. Hentze is a member of national and international academic societies, including the “RNA Society”, the “BioIron Society” (that he co-founded), and the German “Gesellschaft fuer Biochemie und Molekularbiologie (GBM)”.

Public service
Matthias Hentze serves in numerous international advisory functions. He has helped to launch the journals “EMBO Reports” (2000) and “EMBO Molecular Medicine” (2009), and contributes to the editorial boards of “Molecular Cell”, “RNA”, “Trends in Biochemical Sciences”, “Journal of Molecular Medicine” and “EMBO Molecular Medicine”. He is also a member of the Scientific Advisory Boards of the Centro de Biologia Molecular Severo Ochoa (Madrid, Spain), the Spemann Graduate School of Biology and Medicine (Freiburg, Germany), the CIC-Biogune (Bilbao, Spain) and the Queens University Belfast Medical School (Belfast, U.K.).

Selected publications
Matthias Hentze has co-authored textbooks in the field of Molecular Medicine and has contributed over 200 peer-reviewed scientific publications, including


 * Hentze, M.W., S.W. Caughman, T.A. Rouault, J.G. Barriocanal, A. Dancis, J.B. Harford and R.D. Klausner (1987). Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science 238, 1570-1573.


 * Ostareck, D.H., A. Ostareck-Lederer, M. Wilm, B.J. Thiele, M. Mann and M.W. Hentze (1997). mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3’ end. Cell 89, 597-606.


 * Preiss, T. and M.W. Hentze. Dual function of the cap structure in poly(A) tail-promoted translation in yeast (1998). Nature 392, 516-520.


 * Muckenthaler, M., N.K. Gray and M.W. Hentze (1998). IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F. Molecular Cell 2, 383-388.


 * Ostareck, D.H., A. Ostareck-Lederer, I.N. Shatsky and M.W. Hentze (2001). Lipoxygenase mRNA silencing in erythroid differentiation: the 3‘UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104, 281-290.


 * Muckenthaler, M., C.N. Roy, A.O. Custodio, B. Minana, J. deGraaf, L.K. Montross, N.C. Andrews and M.W. Hentze (2003). Regulatory defects in liver and intestine implicate abnormal hepcidin and Cybrd1 expression in mouse hemochromatosis. Nature Genetics 34, 102-107.


 * Hentze, M.W., M.U. Muckenthaler and N.C. Andrews (2004). Balancing acts: molecular control of mammalian iron metabolism. Cell 117, 285-297.


 * Beckmann, K., M. Grskovic, F. Gebauer and M.W. Hentze. A dual inhibitory mechanism restricts msl-2 mRNA translation for dosage compensation in Drosophila (2005). Cell 122, 529-540.


 * Thermann, R. and M.W. Hentze (2007). Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation. Nature 447, 875-879, 2007.


 * Galy, B., D. Ferring-Appel,, S. Kaden, H.-J. Gröne and M.W. Hentze (2008). Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell Metab. 7, 79-85.