Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
5R29GM051140-03
Application #
2189459
Study Section
AIDS and Related Research Study Section 3 (ARRC)
Project Start
1994-05-01
Project End
1999-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Maryland College Park
Department
Microbiology/Immun/Virology
Type
Schools of Earth Sciences/Natur
DUNS #
City
College Park
State
MD
Country
United States
Zip Code
20742
Achuthan, Vasudevan; DeStefano, Jeffrey J (2015) Alternative divalent cations (Zn²?, Co²?, and Mn²?) are not mutagenic at conditions optimal for HIV-1 reverse transcriptase activity. BMC Biochem 16:12
Achuthan, Vasudevan; Keith, Brian J; Connolly, Bernard A et al. (2014) Human immunodeficiency virus reverse transcriptase displays dramatically higher fidelity under physiological magnesium conditions in vitro. J Virol 88:8514-27
Lieberman, Ori J; DeStefano, Jeffrey J; Lee, Vincent T (2013) Detection of cyclic diguanylate G-octaplex assembly and interaction with proteins. PLoS One 8:e53689
Lai, Yi-Tak; DeStefano, Jeffrey J (2012) DNA aptamers to human immunodeficiency virus reverse transcriptase selected by a primer-free SELEX method: characterization and comparison with other aptamers. Nucleic Acid Ther 22:162-76
Nair, Gauri R; Dash, Chandravanu; Le Grice, Stuart F J et al. (2012) Viral reverse transcriptases show selective high affinity binding to DNA-DNA primer-templates that resemble the polypurine tract. PLoS One 7:e41712
Lai, Yi-Tak; DeStefano, Jeffrey J (2011) A primer-free method that selects high-affinity single-stranded DNA aptamers using thermostable RNA ligase. Anal Biochem 414:246-53
Fenstermacher, Katherine J; DeStefano, Jeffrey J (2011) Mechanism of HIV reverse transcriptase inhibition by zinc: formation of a highly stable enzyme-(primer-template) complex with profoundly diminished catalytic activity. J Biol Chem 286:40433-42
Olimpo, Jeffrey T; DeStefano, Jeffrey J (2010) Duplex structural differences and not 2'-hydroxyls explain the more stable binding of HIV-reverse transcriptase to RNA-DNA versus DNA-DNA. Nucleic Acids Res 38:4426-35
Gangaramani, Divya R; Eden, Elizabeth L; Shah, Manthan et al. (2010) The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity. RNA Biol 7:820-9
DeStefano, Jeffrey J (2010) Effect of reaction conditions and 3AB on the mutation rate of poliovirus RNA-dependent RNA polymerase in a alpha-complementation assay. Virus Res 147:53-9