The Interdependency of Drug Resistance Evolution and Drug Design: HIV-1 Protease a Case Study Administrative Core The Administrative Core will provide oversight to the whole Program Project to ensure effective communication and maximum possible synergy between Projects and Cores, and make sure the resources are utilized in the most efficient manner to achieve our common scientific goals. The Administrative Core has the following specific Aims:
Aim 1. Provide leadership to the Program Project's administration including fiscal oversight, and ensure regulatory compliance.
Aim 2. Coordinate and integrate scientific operation of Projects and Cores.
Aim 3. Facilitate communication, synergy and community among the teams.
Aim 4. Manage progress review and strategic planning.
Aim 5. Ensure communication of results with the scientific community, through conferences and publications.

Public Health Relevance

The Interdependency of Drug Resistance Evolution and Drug Design: HIV-1 Protease a Case Study Administrative Core The Administrative Core will provide oversight to the whole Program Project to ensure effective communication and maximum possible synergy between Projects and Cores, and make sure the resources are utilized in the most efficient manner to achieve our common scientific goals.

Agency
National Institute of Health (NIH)
Type
Research Program Projects (P01)
Project #
1P01GM109767-01A1
Application #
8789527
Study Section
Special Emphasis Panel (ZRG1)
Project Start
Project End
Budget Start
Budget End
Support Year
1
Fiscal Year
2014
Total Cost
Indirect Cost
City
Worcester
State
MA
Country
United States
Zip Code
01655
Kurt Yilmaz, Nese; Swanstrom, Ronald; Schiffer, Celia A (2016) Improving Viral Protease Inhibitors to Counter Drug Resistance. Trends Microbiol 24:547-57
Özer, Nevra; Özen, Ayşegül; Schiffer, Celia A et al. (2015) Drug-resistant HIV-1 protease regains functional dynamics through cleavage site coevolution. Evol Appl 8:185-98
Potempa, Marc; Nalivaika, Ellen; Ragland, Debra et al. (2015) A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro. J Mol Biol 427:2360-78
Zhou, Hao; Li, Shangyang; Badger, John et al. (2015) Modulation of HIV protease flexibility by the T80N mutation. Proteins 83:1929-39
Ishima, Rieko (2015) Effects of radiation damping for biomolecular NMR experiments in solution: a hemisphere concept for water suppression. Concepts Magn Reson Part A Bridg Educ Res 44A:252-262
Cai, Yufeng; Myint, Wazo; Paulsen, Janet L et al. (2014) Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 Protease. J Chem Theory Comput 10:3438-3448
Ragland, Debra A; Nalivaika, Ellen A; Nalam, Madhavi N L et al. (2014) Drug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease. J Am Chem Soc 136:11956-63
Kolli, Madhavi; Ozen, Ayşegül; Kurt-Yilmaz, Nese et al. (2014) HIV-1 protease-substrate coevolution in nelfinavir resistance. J Virol 88:7145-54
Özen, Ayşegül; Lin, Kuan-Hung; Kurt Yilmaz, Nese et al. (2014) Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 protease. Proc Natl Acad Sci U S A 111:15993-8