To protect mammals against retroviral infections, TRIM5 restriction factors recognize viral capsids by forming complementary hexagonal nets that can adapt to the patterns of capsid protein subunits on the viral capsid surface.

Folding and unfolding of a 6-helix bundle controls HIV assembly and maturation.

Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.

The examination of the ultra-structure and in vivo dynamics of endocytosis in plants reveal plants unique actin-independent, clathrin-mediated endocytosis mechanisms to overcome their unique physiological properties.

Higher-order assembly enables and links pathogen recognition and downstream steps in the TRIM5-mediated anti-HIV response.

Using both electron cryo-tomography and helical reconstruction, the first structure of the entire archaellum machinery with an assembled filament has been determined, providing the structural basis for our understanding of archaeal motility.

Biochemical and instrumental analysis showed that the membrane-induced exposure of myristoyl from the MA protein of Mason-Pfizer monkey virus triggers allosteric conformational changes resulting in MA oligomerization and unfolding of the cleavage site between MA and downstream domains of Gag.

Interactions were visualized between the nuclear egress complex from herpes simplex virus and a capsid protein that could promote nucleocytoplasmic translocation of the capsid in infected cells.

Small molecule antivirals that drive assembly of HBV capsid protein can also bind to pre-assembled capsids causing them to change morphology or even break, suggesting a complex transduction of binding effects across the capsid.

Formation and cell pole-localization of chemotactic signaling-arrays is a coupled process mediated by ParP, which drives localized array-assembly and regulates the localization-dynamics of its network constituents.