Alex B. Kleinpeter

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.

EZ-DMS provides a simple, cost-effective protocol and software for deep mutational scanning of HIV-1 Env protein variants, enabling analysis of amino acid fitness without bioinformatics expertise.

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.