Evidence map›Paper›PMID 26292704›Full record

ArticleScience (New York, N.Y.)2015

Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex.

Hema Chug, Sergei Trakhanov, Bastian B Hülsmann, Tino Pleiner, Dirk Görlich

Abstract read
PubMed Publisher
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

73 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  5. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  6. Article
  7. Review
  8. Nucleoporin-associated steroid-resistant nephrotic syndrome.Pediatric nephrology (Berlin, Germany) · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Hema ChugDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Sergei TrakhanovDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Bastian B HülsmannDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Tino PleinerDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Dirk GörlichDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. goerlich@mpibpc.mpg.de.
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Here, we report a structural analysis of the FG Nup62•58•54 complex, which is a crucial component of the transport system. It comprises a ≈13 nanometer-long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. We further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general gating of the NPC, are incompatible with the trimer structure. We suggest that the highly elongated Nup62 complex projects barrier-forming FG repeats far into the central NPC channel, supporting a barrier that guards the entire cross section.

Indexed as

AnimalsCrystallography, X-RayDatabases, ProteinNuclear PoreNuclear Pore Complex ProteinsProtein Structure, TertiaryXenopus laevisXenopus ProteinsNuclear Pore Complex ProteinsXenopus Proteins

Identifiers

PMID26292704
OpenAlexW2149115518

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.