The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.
Super-resolution microscopy reveals, at nanometric-scale, the highly organized protein structure of viroplasms, the viral factories used by rotavirus to replicate its genome and assemble new viral particles.
Super-resolution STED microscopy is demonstrated for the first time in the deeply embedded mouse hippocampus in vivo, revealing direct evidence for an unprecedentedly high level of synapse remodeling in a brain structure closely associated with memory processing.
Par-complex-dependent cell polarity can be cell-autonomously conferred to non-polar Drosophila S2 cells, unveiling temporal patterns toward the cortical localization of Par-complex aggregates that include a meshwork containing unit segments.
The Ran GTPase plays a role in defining the physical properties of the nuclear pore complex transport channel by remodeling the binding interactions of importin-β with the nucleoporin Nup153 at the nuclear face of the pore.