ArticleNature nanotechnology2011
Single-molecule transport across an individual biomimetic nuclear pore complex.
Article in Nature nanotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed, 240 citations in OpenAlex.
- Expandable DNA-origami rings as a nanomechanical platform for studying disordered nucleoporins.bioRxiv : the preprint server for biology · 2026Article
- Addressing the Challenges of Solid-State Nanopores: Strategies for Performance Enhancement.International journal of molecular sciences · 2026Review
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- Off-pore Nup98 condensates mobilize heterochromatic breaks and exclude Rad51.Molecular cell · 2025Article
- The Electric Field in Solid State Nanopores Causes Dissociation of Strong Biomolecular Interactions.Nano letters · 2025Article
- Solid-State Nanopore Sensors: Analyte Quantification by Event Frequency Analysis at High Voltages.Analytical chemistry · 2025Article
- Nanopore approaches for single-molecule temporal omics: promises and challenges.Nature methods · 2025Review
- Coacervate-pore complexes for selective molecular transport and dynamic reconfiguration.Nature communications · 2024Article
- Channel width modulates the permeability of DNA origami-based nuclear pore mimics.Science advances · 2024Article
- Channel width modulates the permeability of DNA origami based nuclear pore mimics.bioRxiv : the preprint server for biology · 2024Article
- Diameter dependence of transport through nuclear pore complex mimics studied using optical nanopores.eLife · 2024Article
- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- Confirming Silent Translocation through Nanopores with Simultaneous Single-Molecule Fluorescence and Single-Channel Electrical Recordings.Analytical chemistry · 2023Article
- A survey of the specificity and mechanism of 1,6 hexanediol-induced disruption of nuclear transport.Nucleus (Austin, Tex.) · 2023Article
- Dynamics of nuclear export of pre-ribosomal subunits revealed by high-speed single-molecule microscopy in live cells.iScience · 2023Article
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Pore performance: artificial nanoscale constructs that mimic the biomolecular transport of the nuclear pore complex.Nanoscale advances · 2022Review
- Facile Fabrication of Flexible Polymeric Membranes with Micro and Nano Apertures over Large Areas.Polymers · 2022Article
- Blocker Effect on Diffusion Resistance of a Membrane Channel: Dependence on the Blocker Geometry.The journal of physical chemistry. B · 2022Article
37 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes regulate the selective exchange of RNA and proteins across the nuclear envelope in eukaryotic cells. Biomimetic strategies offer new opportunities to investigate this remarkable transport phenomenon. Here, we show selective transport of proteins across individual biomimetic nuclear pore complexes at the single-molecule level. Each biomimetic complex is constructed by covalently tethering either Nup98 or Nup153 (phenylalanine-glycine (FG) nucleoporins) to a solid-state nanopore. Individual translocation events are monitored using ionic current measurements with sub-millisecond temporal resolution. Transport receptors (Impβ) proceed with a dwell time of ∼2.5 ms for both Nup98- and Nup153-coated pores, whereas the passage of non-specific proteins is strongly inhibited with different degrees of selectivity. For pores up to ∼25 nm in diameter, Nups form a dense and low-conducting barrier, whereas they adopt a more open structure in larger pores. Our biomimetic nuclear pore complex provides a quantitative platform for studying nucleocytoplasmic transport phenomena at the single-molecule level in vitro.
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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.