American Philosophical Society
Member History

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Resident[X]
Class
Subdivision
201. Molecular Biology and Biochemistry[X]
1Name:  Dr. Tony Hunter
 Institution:  The Salk Institute
 Year Elected:  2006
 Class:  2. Biological Sciences
 Subdivision:  201. Molecular Biology and Biochemistry
 Residency:  Resident
 Living? :   Living
 Birth Date:  1943
   
 
Tony Hunter was born in Ashford, Kent, England. He attended Caius College at the University of Cambridge, receiving his B.A. in 1965. Subsequently, he did his graduate studies in the Department of Biochemistry at the University of Cambridge under the supervision of Asher Korner, receiving his Ph.D. in 1969 for work on mammalian protein synthesis. In 1968 he was appointed as a Research Fellow of Christ's College at the University of Cambridge, and then worked for three years in the Department of Biochemistry doing independent research on the initiation of protein synthesis in eukaryotes. In 1971 he joined the Salk Institute in La Jolla, California, as a Research Associate working under Walter Eckhart on polyoma virus DNA synthesis. He spent 1973-75 back at the Department of Biochemistry at the University of Cambridge where he discovered how tobacco mosaic virus expresses its coat protein, before joining the Salk Institute as an assistant professor in 1975. At that time he set out to identify tumor virus transforming gene products, starting with the tumor (T) antigens of polyoma virus and then turning his attention to Rous sarcoma virus (RSV). In the course of studying the polyoma virus middle T antigen and the RSV v-src gene product, he discovered that these proteins both exhibit a previously unknown protein kinase activity that phosphorylates tyrosine. He has spent most of the last thirty years studying tyrosine kinases and their role in cell growth, oncogenesis and the cell cycle. A major current research interest is to elucidate mechanisms of transmembrane signaling by tyrosine kinases and phosphatases. His group also studies the cyclin-dependent protein kinases and other protein kinases that regulate progression through the cell cycle, and how protein ubiquitylation and degradation is used as a means of regulating signaling pathways and the cell cycle. He is currently a professor in the Molecular and Cell Biology Laboratory at the Salk Institute, the director of the Salk Institute Cancer Center, and an adjunct professor in the Division of Biology at the University of California, San Diego. Currently 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. He serves on a number of scientific review and advisory committees. He has been an organizer for many scientific meetings. He was elected as a Fellow of the Royal Society of London in 1987, a Fellow of the American Academy of Arts & Sciences in 1992, an Associate Member of the European Molecular Biology Organization in 1992, a member of the U.S. National Academy of Sciences in 1998 and a member of the Institute of Medicine in 2004. He was appointed as an American Cancer Society Research Professor in 1992. He has received a number of awards for his work in the area of growth control, oncogenesis and protein phosphorylation, including the 1994 General Motors Cancer Research Foundation Mott Prize, a 1994 Gairdner Foundation International Award, the Biochemical Society 1994 Hopkins Memorial Lectureship and Medal, the 2001 Keio Medical Science Prize, the 2003 Sergio Lombroso Award in Cancer Research, the 2003 City of Medicine Award, the 2004 American Cancer Society Medal of Honor, the 2004 Kirk A. Landon-AACR Prize for Basic Cancer Research, the Prince of Asturias Award for Scientific and Technical Research, 2004, the 2004 Louia Gross Horwitz Prize, the 2005 Wolf Prize in Medicine, the 2006 Pasarow Award in Cancer Research, in 2017 the inaugural Sjoeberg Prize cancer research; the 2018 Pezcoller-AACR International Award for Extraordinary Achievement in Cancer Research, and the 2018 Tang Prize in Biopharmaceutical Science. His hobbies include white water rafting and desert camping.
 
2Name:  Dr. Paul C. Zamecnik
 Institution:  Massachusetts General Hospital, Harvard Medical School
 Year Elected:  2006
 Class:  2. Biological Sciences
 Subdivision:  201. Molecular Biology and Biochemistry
 Residency:  Resident
 Living? :   Deceased
 Birth Date:  1912
 Death Date:  October 27, 2009
   
 
Paul Zamecnik is a senior scientist at Massachusetts General Hospital and Professor Emeritus at Harvard Medical School. He has been affiliated with both institutions for over fifty years and received his M.D. from Harvard Medical School in 1936. Dr. Zamecnik's first great scientific contribution was elucidating important aspects of the biochemistry of protein synthesis. He showed that ATP is necessary for peptide bond formation, which therefore is not a reversal of proteolysis; in the cell free system, he devised the ribosome is the site of these reactions; and tRNAs translate sequences of DNA to protein. Early, he performed RNA sequencing that showed 3'-poly A in Rous sarcoma virus RNA, and a prior sequence identical to that at the 5' end, indicating circular structure. His second greatest contribution was the conception of competitive antisense nucleotides. These blocked virus replication by inhibition of translation. He demonstrated the antisense effect with hemoglobin protein synthesizing cells showing that this depends on the ability of deoxynucleotides to enter intact cells and on Watson-Crick base pairing. He has also applied the concept to medicine, targeting the tuberculosis bacterium and the defective cystic fibrosis gene. A three-time winner of the John Collins Warren Triennial Prize, (1946, 1950, 1999) as well as the Presidential Medal of Science (1991), the Lasker Award (1995) and the Institute of Virology's Lifetime Achievement Award (2004), Dr. Zamecnik was elected to the membership of the American Academy of Arts & Sciences in 1954, the National Academy of Sciences in 1968 and the American Philosophical Society in 2006.
 
Election Year
2006[X]