Eric O. Freed

This study uses MAS NMR to determine the binding mode of HRF-4467, a second-generation HIV-1 maturation inhibitor, in the CA-SP1-NC11 complex with IP6, revealing its mechanism of action and resistance profile.

This study uses single-molecule imaging to show that maturation inhibitors alter Gag conformational dynamics and spatial heterogeneity in immature HIV-1 virions.

This study shows that the central pore of HIV-1 capsomers, mediated by R18 and K25 rings, is critical for capsid stability and post-entry events, with the N21K mutation compensating for R18 loss.

The paper introduces a mechanism-aware platform to determine functional viral enzyme thresholds, revealing differences in stoichiometric requirements and enabling antiviral hypersensitivity detection.

This study identifies PLSCR1 as a host restriction factor that inhibits HIV-1 and related viruses by blocking membrane fusion during entry, independent of interferon signaling.

The paper shows HIV-1 NC mutations accelerate viral DNA integration and reduce INSTI sensitivity, acting with IN mutations to confer resistance.

This study determines the atomic structure of HIV-1 CACTD-SP1 assemblies with PF-46396 and IP6 using MAS NMR, revealing binding modes and IP6 dynamics.

This study shows that an ordered mature MA lattice is not required for HIV-1 infectivity, as a triple mutant lacking this structure remains infectious.

This paper investigates how the M66I mutation in HIV-1 capsid protein confers resistance to lenacapavir by altering inhibitor binding and viral replication.

This paper identifies a mutation, G225R, that restores capsid formation and infectivity to HIV-1 mutants deficient in IP6 packaging by stabilizing the capsid structure in low-IP6 conditions.

This study identifies PSGL-1's decameric repeats as critical for excluding HIV Env from virions through structural folding that spatially hinders Env incorporation.