ArticleeLife2018
Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Threading of Single Protein Molecules Through a Solid-State Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026Article
- 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
- 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
- A Coarse-Grained MD Model for Disorder-To-Order Transitions in PolyQ Aggregation.Journal of chemical theory and computation · 2025Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- C9orf72 polyPR interaction with the nuclear pore complex.Biophysical journal · 2024Article
- Article
- Diameter dependence of transport through nuclear pore complex mimics studied using optical nanopores.eLife · 2024Article
- Phase separation of intrinsically disordered FG-Nups is driven by highly dynamic FG motifs.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.International journal of molecular sciences · 2023Article
- Morphology of Polymer Brushes in the Presence of Attractive Nanoparticles: Effects of Temperature.International journal of molecular sciences · 2023Article
- Molecular basis of C9orf72 poly-PR interference with the β-karyopherin family of nuclear transport receptors.Scientific reports · 2022Article
- Pore performance: artificial nanoscale constructs that mimic the biomolecular transport of the nuclear pore complex.Nanoscale advances · 2022Review
- A simple thermodynamic description of phase separation of Nup98 FG domains.Nature communications · 2022Article
- Super-resolved 3D tracking of cargo transport through nuclear pore complexes.Nature cell biology · 2022Article
- Structure and dynamics of nanoconfined water and aqueous solutions.The European physical journal. E, Soft matter · 2021Review
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Nuclear pore complexes (NPCs) lined with intrinsically disordered FG-domains act as selective gatekeepers for molecular transport between the nucleus and the cytoplasm in eukaryotic cells. The underlying physical mechanism of the intriguing selectivity is still under debate. Here, we probe the transport of ions and transport receptors through biomimetic NPCs consisting of Nsp1 domains attached to the inner surface of solid-state nanopores. We examine both wildtype FG-domains and hydrophilic SG-mutants. FG-nanopores showed a clear selectivity as transport receptors can translocate across the pore whereas other proteins cannot. SG mutant pores lack such selectivity. To unravel this striking difference, we present coarse-grained molecular dynamics simulations that reveal that FG-pores exhibit a high-density, nonuniform protein distribution, in contrast to a uniform and significantly less-dense protein distribution in the SG-mutant. We conclude that the sequence-dependent density distribution of disordered proteins inside the NPC plays a key role for its conductivity and selective permeability.
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Registered trials
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.