Biochemistry and Molecular Biology
Insitute for Bioscience and Biotechnology Research
Education and Training
- Moscow Institute of Physics and Technology, BS, Physics, 1993
- Moscow Institute of Physics and Technology, MS, Physics, 1993
- Institute of Theoretical and Experimental Biophysics, PhD, Biophysics, 1998
- Northwestern University, Postdoctoral Fellow, Membrane biophysics, 2001
- Brandeis University, Postdoctoral Fellow, Structural Biology, 2006
Dr. Pozharskiy received his Ph.D. in 1998 from the Institute of Theoretical and Experimental Biophysics of Russian Academy of Sciences, and initially trained as a postdoctoral fellow in the Department of Biochemistry of Northwestern University. He then pursued postdoctoral training in X-ray crystallography in Rosenstiel Basic Medical research Center at Brandeis University. Dr Pozharskiy was an assistant professor in the Department of Pharmaceutical Sciences of University of Maryland School of Pharmacy and joined joined the Department in 2013 as a member of Center for Biomolecular Therapeutics. He holds concurrent appointment as a Fellow at the Institute for Biosciences and Biotechnology Research.
Dr Pozharskiy's area of scientific expertise is structural biology, with major focus on protein X-ray crystallography. Throughout his career as a protein crystallographer, he has focused on structural mechanisms of molecular recognition in variety of biomolecular systems, including small molecules, protein-DNA and protein-protein interactions. He has also contributed to methodological aspects of protein crystallography, including computational methods, structure validation, and crystallization methods.
Protein crystallography, structure based drug design, biomolecular recognition
Lin J., E. Pozharski , and M.A. Wilson. Short Carboxylic Acid-Carboxylate Hydrogen Bonds Can Have Fully Localized Protons. Biochemistry. 2017, ;56(2):391-402. PMID:27989121.
Coey, C.T., S.S. Malik, K.M. Varney, E. Pozharski, and A.C. Drohat. Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues. Nucleic Acids Research, 2016, 44(21): 10248-10258. PMID:27580719.
Pozharski E, C.X. Weichenberger,and B. Rupp. Techniques, tools and best practices for ligand electron-density analysis and results from their application to deposited crystal structures. Acta Crystallogr D Biol Crystallogr. 2013 69:150-167. PMID:2338545225.
West A.L., S.E. Evans, J.M. González, L.G. Carter, H. Tsuruta, E. Pozharski, and S.L. Michel. Ni(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect. Proc Natl Acad Sci USA. 2012 109(15):5633-5638. PMID:22451934.
Maiti, A., M.T. Morgan, E. Pozharski, and A.C. Drohat, Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition. Proc Natl Acad Sci USA, 2008. 105(26): 8890-8895. PMID: 18587051.