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| Name |
Hunter, Tony |
| Location
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Salk Institute for Biological Studies |
| Primary Field
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Medical Genetics, Hematology and Oncology |
| Secondary Field
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Biochemistry |
 Election Citation
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Hunter is a biochemist from the United Kingdom. He was the first to identify phosphotyrosine protein modifications and the prototypic tyrosine protein kinase. This work stimulated all of the many subsequent studies that have elucidated the fundamental role of these protein kinases in cellular signal transduction, growth control, and morphogenesis.
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Research Interests
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The Hunter group's main focus is on the role of protein phosphorylation in regulating cellular signaling events, and how aberrant phosphorylation causes cancer. His group also works on other types of post-translational modi?cations (PTMs), including ubiquitylation, where he discovered the RING domain class of E3 Ub ligases, and sumoylation, where he identified a class of E3 ubiquitin ligases, STUbLs, that specifically target sumoylated proteins for ubiquitylation. For the past few years, he has been studying histidine phosphorylation of proteins, and has generated monoclonal antibodies specific for the two isoforms of phosphohistidine, which he used to identify many new histidine phosphorylated proteins, and to uncover a possible role for histidine phosphorylation in liver cancer. Most recently, he has investigated the role of stromal cells in pancreatic cancer, discovering a role for the leukemia inhibitory factor (LIF) cytokine secreted by cancer-associated fibroblasts in tumor progression.
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