Juan S. Rey

The paper determines the structure of HIV-1 capsid lattice bound to MxB N-terminal fragment, revealing an alpha-helix stabilizes binding at the trimer interface.

This study shows that CypA binding to HIV-1 capsids affects their mechanical properties, with higher stoichiometry increasing brittleness and reducing deformability.

The paper introduces a geometric criterion to quantify deviations in HIV-1 capsid structure from idealized models and links these deviations to biophysical properties and function.

This study investigates how Lenacapavir disrupts HIV-1 assembly and maturation, revealing a 'premature' lattice formation that prevents infectious virus production.

This study determines high-resolution structures of immature HIV-1 particles with inhibitors BVM and LEN bound using cryo-EM, revealing their distinct binding mechanisms and effects on Gag lattice architecture.

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 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 paper identifies the mechanism of resistance to the HIV-1 integrase inhibitor pirmitegravir and develops a more potent analog to overcome this resistance.