Evidence map›Paper›PMID 35177819›Full record

ArticleCell research2022

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

Gaoxingyu Huang, Xiechao Zhan, Chao Zeng, Xuechen Zhu, Ke Liang, 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Non-classical functions of nuclear pore proteins in ciliopathy.Frontiers in molecular biosciences · 2023
    Review
  16. Article
  17. Article
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, 18 Shilongshan Road, Hangzhou, Zhejiang, China. huanggaoxingyu@westlake.edu.cn.
Xiechao Zhan *Westlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China.
Chao Zeng *Westlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China.
Xuechen Zhu *Westlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China.
Ke Liang *Westlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China.
Yanyu ZhaoWestlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China.
Pan WangBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Tsinghua University, Beijing, China.
Qifan WangWestlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China.
Qiang ZhouWestlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, 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, Tsinghua University, Beijing, China.
Minhao LiuBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Tsinghua University, Beijing, China.
Jianlin LeiBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0002-9384-8742
Chuangye YanBeijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0001-9338-8048
Yigong ShiWestlake Laboratory of Life Sciences and Biomedicine, 18 Shilongshan Road, Hangzhou, Zhejiang, China. syg@westlake.edu.cn.
Westlake University · CNTsinghua University · CNCenter for Life Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear pore complex (NPC) shuttles cargo across the nuclear envelope. Here we present single-particle cryo-EM structure of the nuclear ring (NR) subunit from Xenopus laevis NPC at an average resolution of 5.6 Å. The NR subunit comprises two 10-membered Y complexes, each with the nucleoporin ELYS closely associating with Nup160 and Nup37 of the long arm. Unlike the cytoplasmic ring (CR) or inner ring (IR), the NR subunit contains only one molecule each of Nup205 and Nup93. Nup205 binds both arms of the Y complexes and interacts with the stem of inner Y complex from the neighboring subunit. Nup93 connects the stems of inner and outer Y complexes within the same NR subunit, and places its N-terminal extended helix into the axial groove of Nup205 from the neighboring subunit. Together with other structural information, we have generated a composite atomic model of the central ring scaffold that includes the NR, IR, and CR. The IR is connected to the two outer rings mainly through Nup155. This model facilitates functional understanding of vertebrate NPC.

Indexed as

Nuclear PoreNuclear Pore Complex ProteinsAnimalsCryoelectron MicroscopyCytoplasmNuclear EnvelopeXenopus laevisXenopus ProteinsNuclear Pore Complex ProteinsNUP155 protein, XenopusXenopus Proteins

Identifiers

PMID35177819
PMCPMC8976044
OpenAlexW4212973632

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.