Evidence map›Paper›PMID 31355338›Full record

ArticleScience advances2019

Cryo-EM structure of TRPC5 at 2.8-Å resolution reveals unique and conserved structural elements essential for channel function.

Jingjing Duan, Jian Li, Gui-Lan Chen, Yan Ge, Jieyu Liu, Kechen Xie, Xiaogang Peng, Wei Zhou, Jianing Zhong, Yixing Zhang and 12 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
8.1field-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

61 citing papers in PubMed, 114 citations in OpenAlex.

  1. Review
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  11. Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel.Nature structural & molecular biology · 2025
    Article
  12. Article
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  14. Thermosensing ability of TRPC5: current knowledge and unsettled questions.The journal of physiological sciences : JPS · 2024
    Review
  15. Article
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  18. Review
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1 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

22 authors at 8 institutions in 2 countries.

Jingjing DuanHuman Aging Research Institute (HARI), School of Life Sciences, Nanchang University, Nanchang, Jiangxi 330031, China.ORCID 0000-0003-2716-2627
Jian LiKey Laboratory of Prevention and Treatment of Cardiovascular and Cerebrovascular Diseases of the Ministry of Education, Gannan Medical University, Ganzhou 341000, China.ORCID 0000-0001-9511-4219
Gui-Lan ChenKey Laboratory of Medical Electrophysiology, Ministry of Education and Sichuan Province and Institute of Cardiovascular Research, Southwest Medical University, Luzhou, Sichuan 646000, China.ORCID 0000-0002-9548-6933
Yan GeKey Laboratory of Medical Electrophysiology, Ministry of Education and Sichuan Province and Institute of Cardiovascular Research, Southwest Medical University, Luzhou, Sichuan 646000, China.
Jieyu LiuKey Laboratory of Medical Electrophysiology, Ministry of Education and Sichuan Province and Institute of Cardiovascular Research, Southwest Medical University, Luzhou, Sichuan 646000, China.
Kechen XieKey Laboratory of Medical Electrophysiology, Ministry of Education and Sichuan Province and Institute of Cardiovascular Research, Southwest Medical University, Luzhou, Sichuan 646000, China.
Xiaogang PengKey Laboratory of Molecular Medicine, The Second Affiliated Hospital of Nanchang University, Nanchang 330006, China.
Wei ZhouKey Laboratory of Molecular Medicine, The Second Affiliated Hospital of Nanchang University, Nanchang 330006, China.
Jianing ZhongCollege of Pharmaceutical Sciences, Gannan Medical University, #1 Yixueyuan Road, Ganzhou, Jiangxi 341000, China.ORCID 0000-0002-2781-3437
Yixing ZhangSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi 330031, China.
Jie XuCollege of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
Changhu XueCollege of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
Bo LiangDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.ORCID 0000-0002-5617-9228
Lan ZhuSchool of Molecular Sciences and Biodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.ORCID 0000-0002-9474-1576
Wei LiuSchool of Molecular Sciences and Biodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.
Cheng ZhangJiangxi Jmerry Biopharmaceutical Co. Ltd, Ganzhou, Jiangxi 341000, China.
Xiao-Li TianHuman Aging Research Institute (HARI), School of Life Sciences, Nanchang University, Nanchang, Jiangxi 330031, China.ORCID 0000-0002-0868-7025
Jianbin WangSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi 330031, China.
David E ClaphamJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA.ORCID 0000-0002-4459-9428
Bo ZengKey Laboratory of Medical Electrophysiology, Ministry of Education and Sichuan Province and Institute of Cardiovascular Research, Southwest Medical University, Luzhou, Sichuan 646000, China.ORCID 0000-0002-3474-3158
Zongli LiHoward Hughes Medical Institute, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-1237-7556
Jin ZhangSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi 330031, China.ORCID 0000-0002-9705-0033
Nanchang University · CNSouthwest Medical University · CNHoward Hughes Medical Institute · USArizona State University · USGannan Medical University · CNOcean University of China · CNEmory University · USJiangxi University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transient receptor potential canonical subfamily member 5 (TRPC5), one of seven mammalian TRPC members, is a nonselective calcium-permeant cation channel. TRPC5 is of considerable interest as a drug target in the treatment of progressive kidney disease, depression, and anxiety. Here, we present the 2.8-Å resolution cryo-electron microscopy (cryo-EM) structure of the mouse TRPC5 (mTRPC5) homotetramer. Comparison of the TRPC5 structure to previously determined structures of other TRPC and TRP channels reveals differences in the extracellular pore domain and in the length of the S3 helix. The disulfide bond at the extracellular side of the pore and a preceding small loop are essential elements for its proper function. This high-resolution structure of mTRPC5, combined with electrophysiology and mutagenesis, provides insight into the lipid modulation and gating mechanisms of the TRPC family of ion channels.

Indexed as

Conserved SequenceCryoelectron MicroscopyAnimalsBinding SitesCationsGadoliniumHEK293 CellsHumansIon Channel GatingKineticsLanthanumLipidsMiceMutationStructure-Activity RelationshipTRPC Cation ChannelsCationsGadoliniumLanthanumLipidsTrpc5 protein, mouseTRPC Cation Channels

Identifiers

PMID31355338
PMCPMC6656536
OpenAlexW2963325195

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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.