Evidence map›Paper›PMID 30082700›Full record

ArticleNature communications2018

Structure of the mouse TRPC4 ion channel.

Jingjing Duan, Jian Li, Bo Zeng, Gui-Lan Chen, Xiaogang Peng, Yixing Zhang, Jianbin Wang, David E Clapham, Zongli Li, Jin Zhang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

81 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel.Nature structural & molecular biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Thermosensing ability of TRPC5: current knowledge and unsettled questions.The journal of physiological sciences : JPS · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. The odyssey of the TR(i)P journey to the cellular membrane.Frontiers in cell and developmental biology · 2024
    Review
  17. Article
  18. Article
  19. Review
  20. Review

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

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 3 institutions in 2 countries.

Jingjing DuanSchool of Basic Medical Sciences, Nanchang University, 330031, Nanchang, Jiangxi, China.
Jian LiSchool of Basic Medical Sciences, Nanchang University, 330031, Nanchang, Jiangxi, China.
Bo ZengKey Laboratory of Medical Electrophysiology, Ministry of Education, and Institute of Cardiovascular Research, Southwest Medical University, 646000, Luzhou, Sichuan, China.ORCID http://orcid.org/0000-0002-3474-3158
Gui-Lan ChenKey Laboratory of Medical Electrophysiology, Ministry of Education, and Institute of Cardiovascular Research, Southwest Medical University, 646000, Luzhou, Sichuan, China.
Xiaogang PengThe Key Laboratory of Molecular Medicine, The Second Affiliated Hospital of Nanchang University, 330006, Nanchang, China.
Yixing ZhangSchool of Basic Medical Sciences, Nanchang University, 330031, Nanchang, Jiangxi, China.
Jianbin WangSchool of Basic Medical Sciences, Nanchang University, 330031, Nanchang, Jiangxi, China.
David E ClaphamHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, 20147, USA.ORCID http://orcid.org/0000-0002-4459-9428
Zongli LiDepartment of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA, 02115, USA. zongli_li@hms.harvard.edu.
Jin ZhangSchool of Basic Medical Sciences, Nanchang University, 330031, Nanchang, Jiangxi, China. zhangxiaokong@hotmail.com.
Nanchang University · CNHoward Hughes Medical Institute · USSouthwest Medical University · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31300949National Natural Science Foundation of China (National Science Foundation of China) 31300965National Natural Science Foundation of China (National Science Foundation of China) 31770795
6 · The paper itself

Abstract

Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally mediated hot and cold sensation to intracellular organellar and primary ciliary signaling. Here we report a cryo-electron microscopy (cryo-EM) structure of TRPC4 in its unliganded (apo) state to an overall resolution of 3.3 Å. The structure reveals a unique architecture with a long pore loop stabilized by a disulfide bond. Beyond the shared tetrameric six-transmembrane fold, the TRPC4 structure deviates from other TRP channels with a unique cytosolic domain. This unique cytosolic N-terminal domain forms extensive aromatic contacts with the TRP and the C-terminal domains. The comparison of our structure with other known TRP structures provides molecular insights into TRPC4 ion selectivity and extends our knowledge of the diversity and evolution of the TRP channels.

Indexed as

AnimalsCryoelectron MicroscopyDisulfidesHEK293 CellsHumansHydrogen-Ion ConcentrationLigandsMiceProtein DomainsProtein FoldingTRPC Cation ChannelsDisulfidesLigandsTRPC4 ion channelTRPC Cation Channels

Identifiers

PMID30082700
PMCPMC6079076
OpenAlexW2949657233

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.