Evidence map›Paper›PMID 29700422›Full record

ArticleCell research2018

Structure of the receptor-activated human TRPC6 and TRPC3 ion channels.

Qinglin Tang, Wenjun Guo, Li Zheng, Jing-Xiang Wu, Meng Liu, Xindi Zhou, Xiaolin Zhang, Lei Chen

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
13.5field-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

109 citing papers in PubMed, 194 citations in OpenAlex.

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  12. Review
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  14. Article
  15. Mechanism of (-)-Englerin A and calcium binding on the human TRPC5 channel.Protein science : a publication of the Protein Society · 2025
    Article
  16. Article
  17. Calcium channels as pharmacological targets for cancer therapy.Clinical and experimental medicine · 2025
    Review
  18. Article
  19. Article
  20. Article

49 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

8 authors at 2 institutions in 1 country.

Qinglin TangState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China.
Wenjun GuoState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China.
Li ZhengDizal Pharmaceutical Company, Jiangsu, China.
Jing-Xiang WuState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China.
Meng LiuDizal Pharmaceutical Company, Jiangsu, China.
Xindi ZhouDizal Pharmaceutical Company, Jiangsu, China.
Xiaolin ZhangDizal Pharmaceutical Company, Jiangsu, China. Xiaolin.Zhang@dizalpharma.com.
Lei ChenState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China. chenlei2016@pku.edu.cn.ORCID http://orcid.org/0000-0002-7619-8311
Peking University · CNBuchang Pharma (China) · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRPC6 and TRPC3 are receptor-activated nonselective cation channels that belong to the family of canonical transient receptor potential (TRPC) channels. They are activated by diacylglycerol, a lipid second messenger. TRPC6 and TRPC3 are involved in many physiological processes and implicated in human genetic diseases. Here we present the structure of human TRPC6 homotetramer in complex with a newly identified high-affinity inhibitor BTDM solved by single-particle cryo-electron microscopy to 3.8 Å resolution. We also present the structure of human TRPC3 at 4.4 Å resolution. These structures show two-layer architectures in which the bell-shaped cytosolic layer holds the transmembrane layer. Extensive inter-subunit interactions of cytosolic domains, including the N-terminal ankyrin repeats and the C-terminal coiled-coil, contribute to the tetramer assembly. The high-affinity inhibitor BTDM wedges between the S5-S6 pore domain and voltage sensor-like domain to inhibit channel opening. Our structures uncover the molecular architecture of TRPC channels and provide a structural basis for understanding the mechanism of these channels.

Indexed as

AnimalsCryoelectron MicroscopyHEK293 CellsHumansProtein DomainsProtein MultimerizationProtein Structure, QuaternarySf9 CellsSpodopteraTRPC6 Cation ChannelTRPC Cation ChannelsTRPC3 cation channelTRPC6 Cation ChannelTRPC6 protein, humanTRPC Cation Channels

Identifiers

PMID29700422
PMCPMC6028632
OpenAlexW2801190461

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.