Dr. Simin Rahighi earned her Ph.D. degree in Structural Biology from the Graduate University for Advanced Studies (Hayama, Japan), in 2009. She then worked as a JSPS postdoctoral fellow at the High Energy Accelerator Research Organization (Tsukuba, Japan) before moving to the Goethe University (Germany) in 2011, where she was awarded a long-term EMBO postdoctoral fellowship. In 2013, Dr. Rahighi joined the Structural Biology Department at Stanford University and worked as a postdoctoral fellow and research associate. While at Stanford, Dr. Rahighi received the Katherine McCormick Advanced Postdoctoral Fellowship.
Dr. Rahighi’s research is focused on the study of ubiquitin signaling pathways in the regulation of cellular functions. Her group takes structural and biochemical approaches for the structure-function analysis of the biomolecules and structure-based drug development.
Rahighi, S., Braunstein, I., Ternette, N., Kessler, B., Kawasaki,M., Kato, M., Matsui, T., Weiss, T. M., Stanhill, A., and Wakatsuki, S. (2016). Selective binding of AIRAPL tandem UIMs to Lys48-linked tri-ubiquitin chains. Structure 24: 412-422.
Fujita, H., Rahighi, S., Akita, M., Kato, R., Sasaki, Y., Wakatsuki, S.,and Iwai, K. (2014). Mechanism underlying IKK activation mediated by the linear ubiquitin chain assembly complex (LUBAC). Mol. Cell Biol. 34 (7): 1322-
Rahighi, S., Ikeda, F., Kawasaki, M., Akutsu, M., Suzuki, N., Kato, R., Kensche, T., Uejima, T., Bloor, S., Komander, D., Randow, F., Wakatsuki, S., and Dikic, I. (2009). Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation. Cell 136, 1098-1109.
American Crystallographic Association (ACA)
American Association of Colleges of Pharmacy (AACP)