Till Böcking

The paper shows how SARS-CoV-2 variants, particularly Omicron, evolved proteolytic controls at the Spike furin cleavage site to enhance transmission while reducing lower respiratory tract pathogenicity.

This study investigates allosteric capsid inhibitors and their resistance mutants, showing they trigger innate immune responses and may reduce HIV-1 transmission.

This study uses molecular simulations to show that lenacapavir disrupts HIV-1 capsid assembly by altering hexamer/pentamer ratios and impairing RNA encapsidation.

The paper identifies a ligand-binding pocket in the HTLV-1 capsid protein essential for infectivity, suggesting it as a potential drug target for anti-capsid therapy.

This study shows that cyclophilin A inhibits HIV-1 nuclear entry in mutants by reducing capsid elasticity, which is reversed by suppressor mutations.

This study shows HIV-1 directly binds dynein to hijack microtubule transport for motility, bypassing traditional cargo adaptors.

This paper introduces an artificial protein motor called Tumbleweed that walks directionally along a DNA track in response to ligand inputs.

This study investigates how designer PPR proteins bind to specific RNA sequences, showing they do not scan longer RNAs and instead rely on diffusion, with implications for their localization in organelles.

This paper designs a DNA origami receptor that enables stable complexes with rapid subunit exchange, demonstrating the system's ability to handle both DNA and protein cargo.

The paper identifies a two-factor authentication mechanism used by the innate immune system to detect low-abundance HIV-1 DNA through PQBP1-mediated capsid recognition and cGAS recruitment.