Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM056609-05
Application #
6494805
Study Section
Project Start
2001-08-01
Project End
2002-07-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
5
Fiscal Year
2001
Total Cost
$131,864
Indirect Cost
Name
Rutgers University
Department
Type
DUNS #
001912864
City
New Brunswick
State
NJ
Country
United States
Zip Code
08901
Wang, Junmei; Kang, Xinshan; Kuntz, Irwin D et al. (2005) Hierarchical database screenings for HIV-1 reverse transcriptase using a pharmacophore model, rigid docking, solvation docking, and MM-PB/SA. J Med Chem 48:2432-44
Sarafianos, Stefan G; Clark Jr, Arthur D; Tuske, Steve et al. (2003) Trapping HIV-1 reverse transcriptase before and after translocation on DNA. J Biol Chem 278:16280-8
Wang, J; Morin, P; Wang, W et al. (2001) Use of MM-PBSA in reproducing the binding free energies to HIV-1 RT of TIBO derivatives and predicting the binding mode to HIV-1 RT of efavirenz by docking and MM-PBSA. J Am Chem Soc 123:5221-30
Boyer, P L; Sarafianos, S G; Arnold, E et al. (2000) Analysis of mutations at positions 115 and 116 in the dNTP binding site of HIV-1 reverse transcriptase. Proc Natl Acad Sci U S A 97:3056-61
Wang, W; Kollman, P A (2000) Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model. J Mol Biol 303:567-82
Wang, J; Kollman, P A; Kuntz, I D (1999) Flexible ligand docking: a multistep strategy approach. Proteins 36:1-19
Wang, J; Dixon, R; Kollman, P A (1999) Ranking ligand binding affinities with avidin: a molecular dynamics-based interaction energy study. Proteins 34:69-81
Wang, W; Wang, J; Kollman, P A (1999) What determines the van der Waals coefficient beta in the LIE (linear interaction energy) method to estimate binding free energies using molecular dynamics simulations? Proteins 34:395-402
Eriksson, M A; Pitera, J; Kollman, P A (1999) Prediction of the binding free energies of new TIBO-like HIV-1 reverse transcriptase inhibitors using a combination of PROFEC, PB/SA, CMC/MD, and free energy calculations. J Med Chem 42:868-81