By linking export and licensing of a piRNA precursor transcript, channel nuclear pore complex subunits Nup54 and Nup58 are specifically required to silence transposons in the Drosophila ovary.

Genetic, proteomic, and structural analyses provide insight into the role of Brl1 during nuclear pore complex biogenesis, suggesting a function in the fusion of outer and inner nuclear membranes.

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.

Nuclear pore complex mimics based on solid-state nanopores show significant selectivity below a diameter of 55 nm, which decreases gradually for larger pore diameters.

Interaction of HIV capsids with the cellular protein cleavage-and-polyadenylation factor 6 at the inner side of nuclear pores promotes nuclear entry of the viral replication complex in primary human macrophages.

Simple biophysical considerations explain the collective behavior of molecularly diverse complex protein assemblies that regulate transport between the nucleus and the cytoplasm in eukaryotic organisms.

Discovery of how cells couple addition of membranes with insertion of nuclear pore complexes to form and grow the nucleus.

The nuclear pore complex is transiently proteolyzed during cell differentiation and the nuclear proteome experience dramatic change.

Biomimetic nanopores reveal that the sequence-dependent spatial distribution of intrinsically disordered proteins plays a crucial role in establishing the selective permeability barrier of the nuclear pore complex.

Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.