Evidence map›Paper›PMID 21647294›Full record

ArticleNucleus (Austin, Tex.)

'Natively unfolded' nucleoporins in nucleocytoplasmic transport: clustered or evenly distributed?

Weidong Yang

Open access · greenAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Review
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

1 author at 1 institution in 1 country.

Weidong YangDepartment of Biological Sciences, Center for Photochemical Sciences, Bowling Green State University, OH, USA. wyang@bgsu.edu
Bowling Green State University · US

Funding

Three-Dimensional Super-Resolution Microscopy Study of Nuclear TransportR01GM097037 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI YANG, WEIDONG · 2011 to 2015
$1.3M
Single-Molecule Three-Dimensional Snapshots of Nuclear TransportR15GM094041 · NIGMS · BOWLING GREEN STATE UNIVERSITY · PI YANG, WEIDONG · 2010 to 2010
$348k
NIGMS NIH HHS GM094041-01NIGMS NIH HHS R01 GM097037NIGMS NIH HHS R15 GM094041
6 · The paper itself

Abstract

The nuclear pore complex (NPC) acts as a selective gate that mediates the bidirectional transport of macromolecules between the cytoplasm and the nucleus of eukaryotic cells. 'Natively unfolded' nucleoporins (Nups) with domains rich in phenylalanine-glycine (FG) repeats form the selective permeability barrier and provide binding sites for mobile transport receptors in the NPC. Understanding the structure and function of the FG-Nups barrier under real-time trafficking conditions is still a formidable challenge due to the dynamic nature of a channeled membranous environment. Recently, we have shown that three-dimensional (3D) density maps of transient interactions between the FG-Nups barrier and a cargo-free or a cargo-bound transport receptor in native NPCs can be obtained by an advanced single-molecule fluorescence microscopy approach. Moreover, we found that these interaction sites are spatially clustered into distinct groups in the periphery around a central axial channel with a diameter of approximately 10-20 nm in the NPC. The 3D distribution of interaction sites may indicate some native properties of the FG-Nups barrier. Here we speculate that the selective permeability barrier in the NPC could be formed by clustered FG-Nups.

Indexed as

Active Transport, Cell NucleusCell NucleusGlycineNuclear PoreNuclear Pore Complex ProteinsPhenylalanineProtein FoldingProtein Structure, TertiaryProtein TransportGlycineNuclear Pore Complex ProteinsPhenylalaninenucleocytoplasmic transportreal-time traffickingsingle-molecule fluorescencesingle-molecule trackingsuper-resolution microscopythree-dimensional distribution

Identifiers

PMID21647294
PMCPMC3104804
OpenAlexW2322262065

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.