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In replicative ageing yeast cells, an age-dependent impediment in proper assembly of nuclear pore complexes is associated with altered nuclear transport.

Mutations conferring resistance to Escherichia coli against the chemotherapy drug gemcitabine can have opposite effects on bacterial drug degradation and therefore can increase or decrease the chemotherapy load on neighboring cancer cells.

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.

Measuring and simulating chromatin dynamics reveals that repositioning of genes to the nuclear pore is neither active nor vectorial, but reduces sub-diffusion and coordinates movement between loci on different chromosomes.

Traumatic injury leads to functional defects in nucleocytoplasmic transport and TDP-43 pathology in multiple model systems.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

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.

Learned expectations allow for a distinct anticipatory distractor representation at the feature but not at the spatial level.

β-Catenin-mediated expansion of nephron progenitors is independent of direct β-catenin/chromatin engagement, while progenitor induction proceeds with a β-catenin-driven switch of repressive TCFL1/TCFL2 to activating TCF7/LEF1 factors on transcriptionally poised enhancers.

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.