Seth Robia, PhD

Cell and Molecular Physiology

Professor
Co-Director, Cardiovascular Research Institute,Program Director, Advanced Non-Linear Imaging

Languages Spoken

English

Biography

Biography

Seth Louis Robia, Ph.D., is a Professor in the Department of Cell and Molecular Physiology, Loyola University Chicago. He is also a Co-Director of the Cardiovascular Research Institute. In this capacity Dr. Robia facilitates collaborative research on cardiovascular disease in the Loyola University Chicago Health Sciences Division. Dr. Robia’s role is to bring basic scientists and clinicians together to enhance the translation of fundamental discoveries into practical advances in clinical medicine. Dr. Robia teaches cardiac physiology for Master of Science in Medical Physiology graduate students and for first year medical students in the Stritch School of Medicine.

Dr. Robia received his Bachelor of Arts from St. Olaf College in Northfield, Minnesota, where he majored in Chemistry and Biology. He obtained his M.S. and Ph.D. degrees in the Physiology program at the University of Wisconsin-Madison, then pursued postdoctoral research training at the University of Minnesota. He joined the faculty at Loyola as an Assistant Professor in 2006.
Research in the Robia lab focuses primarily on membrane transport proteins that are important for cell signaling. To discover new information about cellular transport processes, Dr. Robia uses a variety of biophysical methods including fluorescence microscopy, spectroscopy, and computational modeling.

Seth has been married to Jennifer Robia since 1996, and they have 4 children: Samuel, Ella, Lucy, and Benjamin. They live in Westchester, Illinois.

Medical Education

Medical School

Board Certification

Research

  • Dynamic conformational changes in the rhesus TRIM5alpha dimer dictate the potency of HIV-1 restriction Lamichhane, R.; Mukherjee, S.; Smolin, N.; Pauszek, R. F., 3rd; Bradley, M.; Sastri, J.; Robia, S. L.; Millar, D.; Campbell, E. M., Virology
  • Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer Blackwell, D. J.; Zak, T. J.; Robia, S. L., Biophysical journal
  • Restrictive cardiomyopathy Troponin-I R145W mutation does not perturb myofilament length dependent activation in human cardiac sarcomeres Dvornikov, A. V.; Smolin, N.; Zhang, M.; Martin, J. L.; Robia, S. L.; de Tombe, P. P., The Journal of biological chemistry
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  • A Structural Mechanism for Calcium Transporter Headpiece Closure Smolin, N.; Robia, S. L., The journal of physical chemistry.B
  • ABC Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-throughput Screening Iram, S. H.; Gruber, S. J.; Raguimova, O. N.; Thomas, D. D.; Robia, S. L., Molecular pharmacology
  • Acute Inotropic and Lusitropic Effects of Cardiomyopathic R9C Mutation of Phospholamban Abrol, N.; de Tombe, P. P.; Robia, S. L., The Journal of biological chemistry
  • ATP-Binding Cassette Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-Throughput Screening Iram, S. H.; Gruber, S. J.; Raguimova, O. N.; Thomas, D. D.; Robia, S. L., Molecular pharmacology
  • Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex Using Non-Coding RNA and Single-Stranded DNA oligonucleotides Soller, K. J.; Verardi, R.; Jing, M.; Abrol, N.; Yang, J.; Walsh, N.; Vostrikov, V. V.; Robia, S. L.; Bowser, M. T.; Veglia, G., Scientific reports
  • Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex Abrol, N.; Smolin, N.; Armanious, G.; Ceholski, D. K.; Trieber, C. A.; Young, H. S.; Robia, S. L., The Journal of biological chemistry
  • Restriction of HIV-1 by rhesus TRIM5alpha is governed by alpha helices in the Linker2 region Sastri, J.; Johnsen, L.; Smolin, N.; Imam, S.; Mukherjee, S.; Lukic, Z.; Brandariz-Nunez, A.; Robia, S. L.; Diaz-Griffero, F.; Wiethoff, C.; Campbell, E. M., Journal of virology
  • Phosphorylated Phospholamban Stabilizes a Compact Conformation of the Cardiac Calcium-ATPase Pallikkuth, S.; Blackwell, D. J.; Hu, Z.; Hou, Z.; Zieman, D. T.; Svensson, B.; Thomas, D. D.; Robia, S. L., Biophysical journal
  • Dysferlin forms a dimer mediated by the C2 domains and the transmembrane domain in vitro and in living cells Xu, L.; Pallikkuth, S.; Hou, Z.; Mignery, G. A.; Robia, S. L.; Han, R., PLoS ONE
  • Focal adhesion kinase-related nonkinase inhibits vascular smooth muscle cell invasion by focal adhesion targeting tyrosine 168 phosphorylation, and competition for p130(Cas) binding., Koshman, Y. E.; Chu, M.; Engman, S. J.; Kim, T.; Iyengar, R.; Robia, S. L.; Samarel, A. M., Arteriosclerosis, Thrombosis & Vascular Biology
  • Phospholamban binds with differential affinity to calcium pump conformers. Bidwell, P.; Blackwell, D. J.; Hou, Z.; Zima, A. V.; Robia, S. L., Journal of Biological Chemistry
  • Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase. Song, Q.; Pallikkuth, S.; Bossuyt, J.; Bers, D. M.; Robia, S. L., Journal of Biological Chemistry
  • TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions Lukic, Z.; Hausmann, S.; Sebastian, S.; Rucci, J.; Sastri, J.; Robia, S. L.; Luban, J.; Campbell, E. M., Retrovirology
  • FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells. Koshman, Y. E.; Kim, T.; Chu, M.; Engman, S. J.; Iyengar, R.; Robia, S. L.; Samarel, A. M., Arteriosclerosis, Thrombosis & Vascular Biology
  • p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha. O'Connor, C.; Pertel, T.; Gray, S.; Robia, S. L.; Bakowska, J. C.; Luban, J.; Campbell, E. M., Journal of virology
  • Isoform specificity of the Na/K-ATPase association and regulation by phospholemman. Bossuyt, J.; Despa, S.; Han, F.; Hou, Z.; Robia, S. L.; Lingrel, J. B.; Bers, D. M., Journal of Biological Chemistry
  • The E3 ubiquitin ligase atrophin interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction. Bhandari, D.; Robia, S. L.; Marchese, A., Molecular biology of the cell
  • Phospholamban oligomerization quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells., Kelly, E. M.; Hou, Z.; Bossuyt, J.; Bers, D. M.; Robia, S. L., Journal of Biological Chemistry
  • Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex. Hou, Z.; Kelly, E. M.; Robia, S. L., Journal of Biological Chemistry
  • Forster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex. Robia, S. L.; Campbell, K. S.; Kelly, E. M.; Hou, Z.; Winters, D. L.; Thomas, D. D., Circulation research