ArticleLife science alliance2018
Atomic force microscopy reveals structural variability amongst nuclear pore complexes.
Article in Life science alliance, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- High-Speed Quantitative Nanomechanical Mapping by Photothermal Off-Resonance Atomic Force Microscopy.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Imaging Nuclear Envelopes Using Correlative AFM/Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Simulating structurally variable nuclear pore complexes for microscopy.Bioinformatics (Oxford, England) · 2023Article
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Maximum-likelihood model fitting for quantitative analysis of SMLM data.Nature methods · 2023Article
- Teaching old dogmas new tricks: recent insights into the nuclear import of HIV-1.Current opinion in virology · 2022Review
- Maturation and shuttling of the yeast telomerase RNP: assembling something new using recycled parts.Current genetics · 2022Review
- TopoStats - A program for automated tracing of biomolecules from AFM images.Methods (San Diego, Calif.) · 2021Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- The Role of Capsid in the Early Steps of HIV-1 Infection: New Insights into the Core of the Matter.Viruses · 2021Review
- Interactions of HIV-1 Capsid with Host Factors and Their Implications for Developing Novel Therapeutics.Viruses · 2021Review
- Factors that mold the nuclear landscape of HIV-1 integration.Nucleic acids research · 2021Review
- Nonlinear mechanics of lamin filaments and the meshwork topology build an emergent nuclear lamina.Nature communications · 2020Article
- A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure.Nature communications · 2020Article
- Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.Nature communications · 2020Article
- Nanocompartmentalization of the Nuclear Pore Lumen.Biophysical journal · 2020Article
- Quantification of Biomolecular Dynamics Inside Real and Synthetic Nuclear Pore Complexes Using Time-Resolved Atomic Force Microscopy.ACS nano · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear pore complex (NPC) is a proteinaceous assembly that regulates macromolecular transport into and out of the nucleus. Although the structure of its scaffold is being revealed in increasing detail, its transport functionality depends upon an assembly of intrinsically disordered proteins (called FG-Nups) anchored inside the pore's central channel, which have hitherto eluded structural characterization. Here, using high-resolution atomic force microscopy, we provide a structural and nanomechanical analysis of individual NPCs. Our data highlight the structural diversity and complexity at the nuclear envelope, showing the interplay between the lamina network, actin filaments, and the NPCs. It reveals the dynamic behaviour of NPC scaffolds and displays pores of varying sizes. Of functional importance, the NPC central channel shows large structural diversity, supporting the notion that FG-Nup cohesiveness is in a range that facilitates collective rearrangements at little energetic cost. Finally, different nuclear transport receptors are shown to interact in qualitatively different ways with the FG-Nups, with particularly strong binding of importin-β.
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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.