Evidence map›Paper›PMID 25420031›Full record

ArticleNature nanotechnology2015

Nanoscale stiffness topography reveals structure and mechanics of the transport barrier in intact nuclear pore complexes.

Aizhan Bestembayeva, Armin Kramer, Aksana A Labokha, Dino Osmanović, Ivan Liashkovich, Elena V Orlova, Ian J Ford, Guillaume Charras, Ariberto Fassati, Bart W Hoogenboom

Open access · greenAbstract read
In one paragraph

Article in Nature nanotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Review
  3. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  4. Article
  5. Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. The capsid revolution.Journal of molecular cell biology · 2024
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Aizhan Bestembayeva *London Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, United Kingdom.
Armin Kramer *London Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, United Kingdom.
Aksana A LabokhaWohl Virion Centre, Division of Infection & Immunity, MRC Centre for Medical Molecular Virology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Dino OsmanovićLondon Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, United Kingdom.
Ivan LiashkovichInstitute of Physiology II, University of Münster, Robert-Koch Strasse 27b, 48149 Münster, Germany.
Elena V OrlovaDepartment of Biological Sciences, Birkbeck College, Institute of Structural and Molecular Biology, Malet Street, London WC1E 7HX, United Kingdom.
Ian J FordLondon Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, United Kingdom.
Guillaume CharrasLondon Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, United Kingdom.
Ariberto FassatiWohl Virion Centre, Division of Infection & Immunity, MRC Centre for Medical Molecular Virology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Bart W HoogenboomLondon Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, United Kingdom.
London Centre for Nanotechnology · GBUniversity College London · GBInstitute of Structural and Molecular Biology · GBUniversity of Münster · DE

Funding

Biotechnology and Biological Sciences Research Council BB/G011729/1Medical Research Council G0900950Wellcome Trust 083810Wellcome Trust 083810/Z/07/Z
6 · The paper itself

Abstract

The nuclear pore complex (NPC) is the gate for transport between the cell nucleus and the cytoplasm. Small molecules cross the NPC by passive diffusion, but molecules larger than ∼5 nm must bind to nuclear transport receptors to overcome a selective barrier within the NPC. Although the structure and shape of the cytoplasmic ring of the NPC are relatively well characterized, the selective barrier is situated deep within the central channel of the NPC and depends critically on unstructured nuclear pore proteins, and is therefore not well understood. Here, we show that stiffness topography with sharp atomic force microscopy tips can generate nanoscale cross-sections of the NPC. The cross-sections reveal two distinct structures, a cytoplasmic ring and a central plug structure, which are consistent with the three-dimensional NPC structure derived from electron microscopy. The central plug persists after reactivation of the transport cycle and resultant cargo release, indicating that the plug is an intrinsic part of the NPC barrier. Added nuclear transport receptors accumulate on the intact transport barrier and lead to a homogenization of the barrier stiffness. The observed nanomechanical properties in the NPC indicate the presence of a cohesive barrier to transport and are quantitatively consistent with the presence of a central condensate of nuclear pore proteins in the NPC channel.

Indexed as

Active Transport, Cell NucleusAdhesivenessAdsorptionElastic ModulusFrictionMaterials TestingMicroscopy, Atomic ForceNanoparticlesNuclear PoreStress, MechanicalSurface Properties

Identifiers

PMID25420031
PMCPMC4286247
OpenAlexW1965738455

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Registered trials

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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.