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| Name |
Ahn, Natalie G. |
| Location
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University of Colorado Boulder |
| Primary Field
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Biochemistry |
| Secondary Field
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Biophysics and Computational Biology |
 Election Citation
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Ahn discovered MAP kinase kinases and their activation of MAP kinases, which are essential regulators of signal transduction pathways universal to eukaryotic cells. She pioneered methods and applications of functional proteomics and hydrogen-deuterium exchange mass spectrometry, and used them to elucidate new mechanisms for signaling and enzymatic regulation. |
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Research Interests
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Natalie Ahn's laboratory investigates new mechanisms underlying the regulation and function of cell signaling, by integrating biochemical, biophysical, and cellular strategies with biomolecular analysis by mass spectrometry. Her research examines cell signaling mechanisms involving oncogenic B-Raf/MAPK and Wnt5a pathways, and structural and dynamic properties of protein kinases. Research projects include identification of cellular targets downstream of oncogenic B-Raf/MAPK pathways in cancer, using functional proteomics for large scale protein identification and mapping of protein post-translational modifications. Other projects explore mechanisms underlying a rear-polarized "WRAMP structure" complex assembled in response to the signaling ligand, Wnt5a, which controls directional cell movement through rear-directed Ca2+ signaling and membrane retraction. Finally, biophysical studies combine hydrogen-deuterium exchange mass spectrometry with NMR relaxation and enzyme kinetic measurements to investigate how MAP kinases are regulated at the level of conformational mobility and dynamics, and how this affects the behavior of tight binding kinase inhibitors. |
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