Publications
Recent Publications:
Liu, Z., Wang, Y., Yedidi, R., Dewdney, T.G., Reiter, S.J., Brunzelle, J.S., Kovari, I.A., Kovari, L.C. 2012. Conserved hydrogen bonds and water molecules in MDR HIV-1 protease substrate complexes. Biochem Biophys Res Commun [in press]
Wang, Y., Dewdney, T.G., Liu, Z., Reiter, S.J., Brunzelle, J., Kovari, I.A., Kovari L.C. 2012. Higher desolvation energy reduces molecular recognition in multi-drug resistant HIV-1 protease. Biology 1(1), 81-93; doi:10.3390/biology1010081
Yedidi RS, Liu Z, Wang Y, Brunzelle JS, Kovari IA, Woster PM, L.C. Kovari, Gupta D. 2012. Crystal structures of multidrug-resistant HIV-1 protease in complex with two potent anti-malarial compounds. Biochem Biophys Res Commun 421(3):413-7.
Wang, Y., Dewdney, T.G., Liu, Z., Reiter S.J., Brunzelle, J.S., Kovari, I.A., Kovari L.C. 2011. X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions.Studia UBB Chemia.
Liu, Z., Wang, Y., Yedidi, R.S. Brunzelle, J.S., Kovari, I.A., Sohi, J., Kamholz, J., and L.C. Kovari. 2012. Crystal structure of the extracellular domain of human myelin protein zero. Proteins. doi: 10.1002/prot.23164. [Epub ahead of print].
Wang, Y., Liu, Z., Brunzelle, J.S., Kovari, I.A., Dewdney, T.G., Reiter, S.J., and L.C. Kovari. 2011. The higher barrier of darunavir and tipranavir resistance for HIV-1 protease. Biochem Biophys Res Commun 412(4): 737-42.
Yedidi, R.S., Proteasa G., Martinez, J.L., Vickrey, J.F., Martin, P.D., Wawrzak, Z., Liu, Z., Kovari, I.A., and L.C. Kovari. 2011. Contribution of the 80s loop of HIV-1 protease to the multidrug-resistance mechanism: crystallographic studies of MDR769 HIV-1 protease variants. Acta Crystallogr D Biol Crystallogr 67(Pt 6): 524-32.
Liu, Z., Wang, Y., Brunzelle, J., Kovari, I.A., and L.C. Kovari. 2011. Nine crystal structures determine the substrate envelope of the MDR HIV-1 protease. Protein J (3): 173-83.
Gupta, D., Yedidi R.D., Varghese, S., L.C. Kovari, and Woster, P.M. 2010. Mechainsm-based inhibitors of the aspartyl protease plasmepsin II as potential antimalarial agents. J Med Chem 53(10): 4234-47.
Martin, P., J. F. Vickrey, G. Proteasa, Y. L. Jimenez, Z. Wawrzak, M. A. Winters, T. C. Merigan, and L. C. Kovari. 2005. "Wide-open" 1.3 A structure of a multidrug-resistant HIV-1 protease as a drug target. Structure 13:1887-95
Logsdon, B. C., J. F. Vickrey, P. Martin, G. Proteasa, J. I. Koepke, S. R. Terlecky, Z. Wawrzak, M. A. Winters, T. C. Merigan, and L. C. Kovari. 2004. Crystal structures of a multidrug-resistant human immunodeficiency virus type 1 protease reveal an expanded active-site cavity. J Virol 78:3123-32.
Vickrey, J. F., B. C. Logsdon, G. Proteasa, S. Palmer, M. A. Winters, T. C. Merigan, and L. C. Kovari. 2003. HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization. Protein Expr Purif 28:165-72.
Holland-Staley, C. A., L. C. Kovari, E. M. Golenberg, K. J. Pobursky, and D. L. Mayers. 2002. Genetic diversity and response to IFN of the NS3 protease gene from clinical strains of the hepatitis C virus. Arch Virol 147:1385-406.
Winters, M. A., K. L. Coolley, P. Cheng, Y. A. Girard, H. Hamdan, L. C. Kovari, and T. C. Merigan. 2000. Genotypic, phenotypic, and modeling studies of a deletion in the beta3-beta4 region of the human immunodeficiency virus type 1 reverse transcriptase gene that is associated with resistance to nucleoside reverse transcriptase inhibitors. J Virol 74:10707-13.
Kovari, L. C., C. A. Momany, F. Miyagi, S. Lee, S. Campbell, B. Vuong, V. M. Vogt, and M. G. Rossmann. 1997. Crystals of Rous sarcoma virus capsid protein show a helical arrangement of protein subunits. Virology 238:79-84.
Momany, C., L. C. Kovari, A. J. Prongay, W. Keller, R. K. Gitti, B. M. Lee, A. E. Gorbalenya, L. Tong, J. McClure, L. S. Ehrlich, M. F. Summers, C. Carter, and M. G. Rossmann. 1996. Crystal structure of dimeric HIV-1 capsid protein. Nat Struct Biol 3:763-70.
Kovari, L. C., C. Momany, and M. G. Rossmann. 1995. The use of antibody fragments for crystallization and structure determinations. Structure 3:1291-3.