Eda Koculi

Biography

Education: May 2006: Doctor of Philosophy in Biophysics, The Johns Hopkins University. May 1999: Master of Science in Biochemistry, University of Oklahoma. Aug. 1996: Bachelor of Science in Chemistry with High Honors, Illinois Institute of Technology. Awards: Jun. 2010: Winner of the Young Investigator Poster Competition at the Biopolymer Gordon Conference, Newport, RI Jun. 2010: Interdepartmental Biological Sciences Postdoctoral Travel Award, Northwestern University, Evanston, IL Mar. 2010: Advancing Biomedical Research Workforce Diversity: NIGMS Workshop for Postdocs Transitioning to Independent Positions, Bethesda, MD Mar. 2007 - Oct. 2008: Ruth L. Kirschstein National Research Service Award, National Institutes of Health Mar. 2002: J. Brein Key Graduate Student Assistant Fund, The Johns Hopkins University, Baltimore, MD Aug. 1994 - May 1995: Energy Environment Economy Scholarship, Illinois Institute of Technology, Chicago, IL Aug. 1993 - May 1994: Flood Scholarship, Illinois Institute of Technology, Chicago, IL

Research Interest

The research in the Koculi laboratory aims to investigate RNA-protein interactions to understand fundamental biological processes implicated in HIV-1 infection, cancer progression, and bacterial survival. Student and postdoctoral fellows in our laboratory are engaged in multidisciplinary research that combines molecular biology, chemistry, biochemistry and biophysics. The research in our laboratory can be divided in two areas. Regulation of DDX3 Catalytic Activity DDX3 is a human DEAD-box protein that is essential for the export of partially spliced and unspliced HIV-1 transcripts from the nucleus to the cytoplasm, and it is an important regulator of breast cancer metastasis. To design specific inhibitors of DDX3, a molecular understanding is required of how the DDX3 function is regulated. At present, knowledge of this regulatory mechanism is completely missing and it will be one of the major aims of our research. RNA Intermediate Structures on Ribosome Assembly The structural rearrangements that DEAD-box proteins perform during large subunit ribosome assembly are not known. The determination of these structural rearrangements will provide insight into the ribosome assembly process and inform the development of new classes of antibiotics that target the large ribosome subunit assembly pathway. In the present climate of increasingly antibiotic-resistant pathogenic bacteria, the discovery of new antibiotic targets is of paramount importance.