ArticleBiochemical Society transactions2023
Improving the hole picture: towards a consensus on the mechanism of nuclear transport.
Article in Biochemical Society transactions, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli.Genes & development · 2026Article
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.The journal of physical chemistry. B · 2025Article
- Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.Nature communications · 2025Article
- Elucidating the nanoscopic organization and dynamics of the nuclear pore complex.Nucleus (Austin, Tex.) · 2025Article
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.bioRxiv : the preprint server for biology · 2025Article
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nuclear mechanics as a determinant of nuclear pore complex plasticity.Nature cell biology · 2025Review
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.bioRxiv : the preprint server for biology · 2025Article
- Role of pore dilation in molecular transport through the nuclear pore complex: Insights from polymer scaling theory.PLoS computational biology · 2025Article
- The TEMPO integrator: accelerating molecular simulations by temporally multiscale force prediction.Bioinformatics advances · 2025Article
- Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025Review
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Pre-ribosomal particles from nucleoli to cytoplasm.Nucleus (Austin, Tex.) · 2024Review
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Coacervate-pore complexes for selective molecular transport and dynamic reconfiguration.Nature communications · 2024Article
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
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Abstract
Nuclear pore complexes (NPCs) mediate the exchange of materials between the nucleoplasm and cytoplasm, playing a key role in the separation of nucleic acids and proteins into their required compartments. The static structure of the NPC is relatively well defined by recent cryo-EM and other studies. The functional roles of dynamic components in the pore of the NPC, phenylalanyl-glycyl (FG) repeat rich nucleoporins, is less clear because of our limited understanding of highly dynamic protein systems. These proteins form a 'restrained concentrate' which interacts with and concentrates nuclear transport factors (NTRs) to provide facilitated nucleocytoplasmic transport of cargoes. Very rapid on- and off-rates among FG repeats and NTRs supports extremely fast facilitated transport, close to the rate of macromolecular diffusion in cytoplasm, while complexes without specific interactions are entropically excluded, though details on several aspects of the transport mechanism and FG repeat behaviors remain to be resolved. However, as discussed here, new technical approaches combined with more advanced modeling methods will likely provide an improved dynamic description of NPC transport, potentially at the atomic level in the near future. Such advances are likely to be of major benefit in comprehending the roles the malfunctioning NPC plays in cancer, ageing, viral diseases, and neurodegeneration.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.