Evidence map›Paper›PMID 35301439›Full record

ArticleCell research2022

Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex.

Gaoxingyu Huang, Xiechao Zhan, Chao Zeng, Ke Liang, Xuechen Zhu, Yanyu Zhao, Pan Wang, Qifan Wang, Qiang Zhou, Qinghua Tao and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Cell research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  4. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  13. Article
  14. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  15. Review
  16. Article
  17. Review
  18. Non-classical functions of nuclear pore proteins in ciliopathy.Frontiers in molecular biosciences · 2023
    Review
  19. Article
  20. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    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

14 authors at 3 institutions in 1 country.

Gaoxingyu Huang *Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China. huanggaoxingyu@westlake.edu.cn.
Xiechao Zhan *Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
Chao Zeng *Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
Ke Liang *Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
Xuechen Zhu *Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
Yanyu ZhaoWestlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
Pan WangBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China.
Qifan WangWestlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.
Qiang ZhouWestlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0002-6237-8813
Qinghua TaoBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China.
Minhao LiuBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China.
Jianlin LeiBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China.ORCID http://orcid.org/0000-0002-9384-8742
Chuangye YanBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China.
Yigong ShiWestlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China. syg@westlake.edu.cn.
Westlake University · CNBeijing Advanced Sciences and Innovation Center · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy structure of the inner ring (IR) subunit from the Xenopus laevis NPC at an average resolution of 4.2 Å. A homo-dimer of Nup205 resides at the center of the IR subunit, flanked by two molecules of Nup188. Four molecules of Nup93 each places an extended helix into the axial groove of Nup205 or Nup188, together constituting the central scaffold. The channel nucleoporin hetero-trimer of Nup62/58/54 is anchored on the central scaffold. Six Nup155 molecules interact with the central scaffold and together with the NDC1-ALADIN hetero-dimers anchor the IR subunit to the nuclear envelope and to outer rings. The scarce inter-subunit contacts may allow sufficient latitude in conformation and diameter of the IR. Our structure reveals the molecular basis for the IR subunit assembly of a vertebrate NPC.

Indexed as

Nuclear PoreXenopus ProteinsActive Transport, Cell NucleusAnimalsCryoelectron MicroscopyNuclear EnvelopeNuclear Pore Complex ProteinsXenopus laevisNuclear Pore Complex ProteinsNUP155 protein, XenopusXenopus Proteins

Identifiers

PMID35301439
PMCPMC9061766
OpenAlexW4221077980

What OpenQuestion holds

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LicenceCC BY
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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.