Isabella L. Kaufman

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.