Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
1R01AI027690-01
Application #
3141882
Study Section
(ARR)
Project Start
1988-11-01
Project End
1993-10-31
Budget Start
1988-11-01
Budget End
1989-10-31
Support Year
1
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Rutgers University
Department
Type
Organized Research Units
DUNS #
038633251
City
New Brunswick
State
NJ
Country
United States
Zip Code
08901
Lee, Won-Gil; Frey, Kathleen M; Gallardo-Macias, Ricardo et al. (2015) Discovery and crystallography of bicyclic arylaminoazines as potent inhibitors of HIV-1 reverse transcriptase. Bioorg Med Chem Lett 25:4824-7
Vijayan, R S K; Arnold, Eddy; Das, Kalyan (2014) Molecular dynamics study of HIV-1 RT-DNA-nevirapine complexes explains NNRTI inhibition and resistance by connection mutations. Proteins 82:815-29
Abram, Michael E; Ferris, Andrea L; Das, Kalyan et al. (2014) Mutations in HIV-1 reverse transcriptase affect the errors made in a single cycle of viral replication. J Virol 88:7589-601
Bauman, Joseph D; Patel, Disha; Dharia, Chhaya et al. (2013) Detecting allosteric sites of HIV-1 reverse transcriptase by X-ray crystallographic fragment screening. J Med Chem 56:2738-46
Bollini, Mariela; Frey, Kathleen M; Cisneros, José A et al. (2013) Extension into the entrance channel of HIV-1 reverse transcriptase--crystallography and enhanced solubility. Bioorg Med Chem Lett 23:5209-12
Chung, Suhman; Himmel, Daniel M; Jiang, Jian-Kang et al. (2011) Synthesis, activity, and structural analysis of novel ýý-hydroxytropolone inhibitors of human immunodeficiency virus reverse transcriptase-associated ribonuclease H. J Med Chem 54:4462-73
Das, Kalyan; Bandwar, Rajiv P; White, Kirsten L et al. (2009) Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance. J Biol Chem 284:35092-100
Dunn, Linda L; McWilliams, Mary Jane; Das, Kalyan et al. (2009) Mutations in the thumb allow human immunodeficiency virus type 1 reverse transcriptase to be cleaved by protease in virions. J Virol 83:12336-44
Himmel, Daniel M; Maegley, Karen A; Pauly, Tom A et al. (2009) Structure of HIV-1 reverse transcriptase with the inhibitor beta-Thujaplicinol bound at the RNase H active site. Structure 17:1625-1635
Sarafianos, Stefan G; Marchand, Bruno; Das, Kalyan et al. (2009) Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition. J Mol Biol 385:693-713

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