Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM052382-02
Application #
2191379
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1995-05-24
Project End
1999-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
2
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Duke University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
071723621
City
Durham
State
NC
Country
United States
Zip Code
27705
Miller 3rd, Bill R; Beese, Lorena S; Parish, Carol A et al. (2015) The Closing Mechanism of DNA Polymerase I at Atomic Resolution. Structure 23:1609-1620
Hast, Michael A; Nichols, Connie B; Armstrong, Stephanie M et al. (2011) Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens. J Biol Chem 286:35149-62
Fletcher, Steven; Keaney, Erin Pusateri; Cummings, Christopher G et al. (2010) Structure-based design and synthesis of potent, ethylenediamine-based, mammalian farnesyltransferase inhibitors as anticancer agents. J Med Chem 53:6867-88
Hast, Michael A; Fletcher, Steven; Cummings, Christopher G et al. (2009) Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase. Chem Biol 16:181-92