HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
HIV Dynamics and Replication Program
About Our Program
The HIV Dynamics and Replication Program (HIV DRP) was formed in 1997 as the HIV Drug Resistance Program, with the mission of conducting and fostering multidisciplinary basic, translational, and clinical research focused on problems related to drug-resistant HIV.Â
The scope of research conducted by HIV DRP scientists has expanded over the years to encompass a broader range of important problems in virus biology. Thus, in 2015, the name of the Program was changed to HIV Dynamics and Replication to better capture the breadth of the research carried out by the Program. Read more...
Investigators
Eric O. Freed, Ph.D.
Director
Stephen H. Hughes, Ph.D.
Chief
Alex Compton, Ph.D.
Investigator
Wei-Shau Hu, Ph.D.
Senior Investigator
Mary F. Kearney, Ph.D.
Senior Scientist
Frank Maldarelli, M.D., Ph.D.
Senior Investigator
Vinay K. Pathak, Ph.D.
Senior Investigator
Alan Rein, Ph.D.
Senior Investigator
Zhi-Ming Zheng, M.D., Ph.D.
Senior Investigator
Recent Publications
- Structural mimicry drives HIV-1 Rev-mediated HERV-K expression
- How to package the RNA of HIV-1
- Impact of nuclear export pathway on cytoplasmic HIV-1 RNA transport mechanism and distribution
- Elucidating the basis for permissivity of the MT-4 T-cell line to replication of an HIV-1 mutant lacking the gp41 cytoplasmic tail
- HIV-DRLink: A tool for reporting linked HIV-1 drug resistance mutations in large single-genome datasets using the Stanford HIV Database
- HIV-1 viremia not suppressible by antiretroviral therapy can originate from large T-cell clones producing infectious virus
- Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state
- Crystal structure of a soluble APOBEC3G variant suggests ssDNA to bind in a channel that extends between the two domains
Upcoming Events
Dec
1
2020
Dec
2
2020
Dec
15
2020
Dec
23
2020