Photo of Olga Vinogradova

Olga Vinogradova

  • E-Mail
  • Phone
    • (860) 486-2972
  • Fax
    • (860) 486-6857
  • Office
    • School of Pharmacy
      Room 632
  • Mail
    • University of Connecticut
      Dept. of Pharmaceutical Sciences
      69 North Eagleville Road
      Storrs, CT 06269-3092

Associate Professor of Medicinal Chemistry

Vinogradova Lab Website »


Educational Background

  • M.S. Moscow Institute of Physics and Technology, Applied Physics and Math
  • Ph.D. Case Western Reserve University, Biophysics and Biomedical Engineering
  • Postdoctoral Training: Cleveland Clinic Foundation, Structural Biology

Research Interests

  • Biomolecular NMR and drug design
  • Structural biology and cell signaling
  • Cell adhesion, migration and remodeling
  • Membrane and membrane-associated proteins

Selected Publications

  • Katyal, P., Puthenveetil, R. and Vinogradova, O. (2013) Structural Insights into the Recognition of β3 Integrin Cytoplasmic Tail by SH3 Domain of Src Kinase, Protein Science 22, 1358-65.
  • Puthenveetil, R. and Vinogradova, O. (2013) Optimization of the Design and Preparation of Nanoscale Phospholipid Bilayers for its Application to Solution NMR, Proteins 81, 1222-1231.
  • West, X.Z., Meller, N., Malinin, N.L., Deshmukh, L., Meller, J., Mahabeleshwar, G.H., Weber, M.E., Kerr, B.A., Vinogradova, O., Byzova, T.V. (2012) Integrin β3 crosstalk with VEGFR accommodating tyrosine phosphorylation as a regulatory switch, PLoS One 7, e31071.
  • Deshmukh, L., Meller, N., Alder, N., Byzova, T., Vinogradova, O. (2011) Tyrosine Phosphorylation as a Conformational Switch: A Case Study of Integrin β3 Cytoplasmic Tail, J. Biol. Chem. 47, 40943-53.
  • Deshmukh, L., Gorbatyuk, V., Vinogradova, O. (2010) Integrin β3 Phosphorylation Dictates its Complex with Shc PTB Domain, J. Biol. Chem. 285, 34875-84.
  • Tyukhtenko, S., Deshmukh, L., Kumar, V., Lary, J., Cole, J., Lemmon, V., Vinogradova, O. (2008) Characterization of neuron specific L1-CAM cytoplasmic tail: Naturally disordered in solution it exercises different binding modes for different adaptor proteins, Biochemistry 47, 4160-4168.