Daniel DiMaio

This study uses cryo-EM and computational methods to model the structure of HPV16 L2 protein within the capsid, revealing its conformational flexibility and positioning for virus entry.

The paper identifies SNX12 as a retromer adaptor critical for HPV16 infection and shows how cargo-adaptor interactions specify retromer coat architecture through structural and functional analyses.

This study shows that importin-7 facilitates HPV transport from the Golgi to the nucleus, promoting infection by binding to the HPV capsid protein L2.

This study shows that γ-secretase interaction with retromer enhances retromer-mediated retrograde transport of specific cargos in human cells.

This study identifies Rab6a as essential for HPV trafficking from the TGN to the nucleus by facilitating its association with dynein and BICD2.