6,742 results found
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner

    Alan R Lowe et al.
    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.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Investigating molecular crowding within nuclear pores using polarization-PALM

    Guo Fu et al.
    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.
    1. Cell Biology

    Age-dependent deterioration of nuclear pore assembly in mitotic cells decreases transport dynamics

    Irina L Rempel et al.
    In replicative ageing yeast cells, an age-dependent impediment in proper assembly of nuclear pore complexes is associated with altered nuclear transport.
  1. Nuclear pore assembly proceeds by an inside-out extrusion of the nuclear envelope

    Shotaro Otsuka et al.
    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.
    1. Cell Biology

    Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore

    Xun X Bao et al.
    Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.
    1. Structural Biology and Molecular Biophysics

    Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics

    Adithya N Ananth et al.
    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.
    1. Cell Biology
    2. Microbiology and Infectious Disease

    HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex

    David Alejandro Bejarano et al.
    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.
    1. Physics of Living Systems
    2. Computational and Systems Biology

    Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex

    Andrei Vovk et al.
    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.
    1. Cell Biology
    2. Microbiology and Infectious Disease

    Nuclear pore heterogeneity influences HIV-1 infection and the antiviral activity of MX2

    Melissa Kane et al.
    Comprehensive investigation reveals the variability and importance of the nuclear pore complex in HIV-1 infection and the activity of the antiretroviral protein, MX2.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity

    Hermann Broder Schmidt, Dirk Görlich
    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.

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