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.

Comprehensive investigation reveals the variability and importance of the nuclear pore complex in HIV-1 infection and the activity of the antiretroviral protein, MX2.

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.

How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.

Proteins that are low abundant and/or poorly accessible to antibodies can be readily localised with fluorescent streptavidin, when expressed fused to a biotin ligase.

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

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

Acetylation of nuclear basket components, following their interaction with accumulating extrachromosomal DNA circles, drives the reorganization of nuclear pore complexes and the loss of cellular viability associated with replicative ageing.

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.

Structure and simulations reveal SARS-CoV-2 NSP10 is more resistant to genetic variations than other SARS-CoV-2 NSPs and that the presence of mutations conserves structural and dynamic changes in NSP10.