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Louisa Gross Horwitz Prize - 2004>Home Pictures from 2004 ceremony
Tony Hunter
In 1979, his lab discovered that a phosphate can be attached to tyrosine residues in proteins, a discovery that enabled researchers to study tyrosine kinases and their functions in signal transduction, cell growth and development, and cancer and other diseases. Dr. Hunter's and Dr. Pawson's work has led to the development of drugs for halting cancer cell proliferation and has potential for other significant therapies. Dr. Hunter's current research interests include the tyrosine kinases of the Src and growth factor receptor families, as well as the signaling pathways downstream of these tyrosine kinases that regulate cell growth, cell migration and differentiation. His group also studies the cyclin-dependent protein kinases and other protein kinases that regulate progression through the cell cycle, how protein ubiquitination and degradation is used as a means of regulating signaling pathways and the cell cycle, and protein trafficking. He is on the editorial boards of several journals, including Cell, Molecular Cell, the EMBO Journal and the Proceedings of the National Academy of Sciences and has received many awards for his research, including a National Cancer Institute Outstanding Investigator Award. He is a Fellow of the Royal Society of London, an Associate Member of the European Molecular Biology Organization (EMBO), a Fellow of the American Academy of Arts and Sciences, a Foreign Associate of the National Academy of Sciences, and a Member of the Institute of Medicine. He received his Ph.D. in biochemistry from the University of Cambridge, England, for his research on mammalian protein synthesis. Salk Institute - Tony Hunter Molecular and Cell Biology Laboratory website Anthony Pawson
Through an innovative combination of genetic, biochemical and structural experiments, he defined a fundamental molecular language through which cells in the body communicate with one another. His work is important in understanding a number of diseases including cancer, immune deficiencies, cardiovascular disorders and diabetes. Dr. Pawson received his Ph.D. in molecular biology from London University, England, in 1976. He conducted postdoctoral research at the University of California at Berkeley in the late 1970s, where he identified a variety of retroviral oncogene products, and provided early evidence for the role of tyrosine phosphorylation in malignant transformation. He has been at the University of Toronto and the Samuel Lunenfeld Research Institute since 1985. He has received a number of awards including the Gairdner Foundation International Award, the AACR/Pezcoller International Award for Cancer Research, the Heineken Prize for Biochemistry and Biophysics (Royal Netherlands Academy of Arts and Sciences) and the Killam Prize for Health Sciences. He is a Fellow of the Royal Societies of London and Canada, a Foreign Associate of the National Academy of Sciences, an Associate Member of the European Molecular Biology Organization (EMBO), and a recipient of the Order of Canada. Mount Sinai Hospital - Anthony J. Pawson - Intracellular signalling |
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Tony Hunter, Ph.D., is an American Cancer Society Research Professor and director
of the Molecular and Cell Biology Laboratory at the Salk Institute for Biological Studies.
He is also an adjunct professor in the Division of Biological Sciences at the University
of California at San Diego. His research is focused on how cells regulate their growth
and division, and how mutations in genes that regulate growth lead to cancer. 
Anthony Pawson, Ph.D., is a University Professor of the University of Toronto,
Director of Research at the Samuel Lunenfeld Research Institute of Mt. Sinai Hospital,
and a distinguished scientist of the Canadian Institutes for Health Research. He has
spent the last two decades studying the organization of cell regulatory systems and
how cell surface receptors control intracellular signaling pathways, building on his
identification of the phosphotyrosine-binding Src homology 2 (SH2) domain as the prototypic
interaction module. SH2 domains serve as the model for a large family of protein modules
that act in concert to control many aspects of cellular behavior. Since the discovery of
SH2 domains, the number of different modules has grown into the dozens, many of which he
continues to investigate.| CUMC Home Columbia University New York-Presbyterian Hospital Comments Text-Only Version |