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Vitold E. Galkin , PhD

    • Title:
    • Assistant Professor

    • Role:
    • Faculty

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    • I utilize high resolution cryo Electron Microscopy to study cellular polymers that possess helical symmetry such as actin filaments and their complexes with actin binding proteins. One of the key arias of my interest is a mechanism of activation of thin filament by myosin binding protein-C (MyBP-C) which is an essential regulator of cardiac contractility. Mutations in MyBP-C are linked to hypertrophic cardiomyopathy (HCM), a common heart disorder with a prevalence of 1 in 500 people. Also, I’m interested in regulation of contractile ring upon cell division. The contractile ring is comprised of actin and septin filaments. The molecular mechanisms of polymerization of septin proteins which play essential roles in cell division and cellular morphogenesis are still unknown while alterations in the levels of septin isoforms within the cell are linked to many human diseases including cancer and neuropathies.

    • Office Location:
    • Lewis Hall

    • Undergraduate Education:
    • Graduate Education:
    • MS, Saint-Petersburg Technological State, 1995

      PhD, Institute of Cytology, Russian Academy of Sciences in St. Petersburg, 1999

    • Postdoctoral Education:
    • University of Virginia, 2000 to 2006

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    • My laboratory utilizes three dimensional cryo electron microscopy to determine high resolution structures of large macromolecular complexes that cannot be determined by more traditional methods such as crystallography and nuclear magnetic resonance.  My group has full access to the state of the art Titan Krios electron microscope (UVA) equipped with the direct detector and automated image acquisition system. We also use field emission gun JEOL JEM-2100F microscope equipped with the Gatan SC1000 ORIUS CCD camera and cryo stage (ODU). JEOL 1200 EX ll transmission electron microscope equipped with an 11 megapixel AMT digital camera is conveniently located in Lewis Hall (EVMS). Structural studies of actin and its complexes with actin binding proteins have enormous significance in many aspects of human health, from cell motility in metastasis, to cardiac muscle contraction and rearrangements of the actin cytoskeleton during bacterial pathogenesis. Understanding the mechanisms of regulation of the structure and morphogenesis of the contractile ring upon cell division is crucial for understanding of the molecular mechanisms of cytokinesis.

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    • Bio:
    • Assistant Professor, EVMS, 2013-current

      Research Assistant Professor, University of Virginia, 2009-2013

      Research Scientist, University of Virginia, 2006-2009