Alexa A. Snyder

The paper investigates how the F227C mutation in HIV-1 reverse transcriptase increases susceptibility to islatravir, revealing structural and mechanistic insights into this collateral sensitivity.

The paper investigates how HIV-1 resistance mutations enhance susceptibility to tenofovir by analyzing structural and biochemical changes in reverse transcriptase.

This study reports the crystal structure of HIV-1 reverse transcriptase bound to depulfavirine, showing its extended binding conformation and resistance to common mutations, along with combination efficacy with other antivirals.

The paper characterizes structural, biophysical, and virological properties of HIV-1 capsid-targeting antivirals, showing improved potency and stability through chemical modifications of PF74.