Evidence map›Paper›PMID 39994184›Full record

ArticleNature communications2025

Structural insights into transmembrane helix S0 facilitated RyR1 channel gating by Ca

Risheng Wei, Qiang Chen, Lei Zhang, Congcong Liu, Chuang Liu, Chang-Cheng Yin, Hongli Hu

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Cylindrical Crystallization of CaInternational journal of molecular sciences · 2026
    Review
  6. Review
  7. Article
  8. Review
  9. 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

7 authors.

Risheng Wei *Department of Biophysics, School of Basic Medical Sciences, Peking University, Beijing, 100191, China.
Qiang Chen *Kobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen; Shenzhen, Guangdong, 518172, China.
Lei ZhangElectron Microscopy Analysis Laboratory, Medical and Health Analysis Center, Peking University, Beijing, 100191, China.
Congcong LiuInstitute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital; Shenzhen, Guangdong, 518112, China.ORCID http://orcid.org/0000-0002-8675-9100
Chuang LiuCenter for Biological Cryo-EM, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, China. liuchuang2024@hust.edu.cn.ORCID http://orcid.org/0009-0005-3427-1612
Chang-Cheng YinDepartment of Biophysics, School of Basic Medical Sciences, Peking University, Beijing, 100191, China. ccyin@hsc.pku.edu.cn.ORCID http://orcid.org/0000-0001-7748-3205
Hongli HuKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen; Shenzhen, Guangdong, 518172, China. honglihu@cuhk.edu.cn.ORCID http://orcid.org/0000-0003-3658-272X

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31770785National Natural Science Foundation of China (National Science Foundation of China) 31900868National Natural Science Foundation of China (National Science Foundation of China) 32100963
6 · The paper itself

Abstract

The type-1 ryanodine receptor (RyR1) is an intracellular calcium release channel for skeletal muscle excitation-contraction coupling. Previous structural studies showed that the RyR1 activity is modulated by the exogenous regulators including caffeine, ryanodine, PCB-95 and diamide. An additional transmembrane helix, located adjacent to S1 and S4, has been observed in some structures, although its function remains unclear. Here, we report that using a mild purification procedure, this helix is co-purified with RyR1 and is designated as S0. When RyR1 is coupled with S0, it can be activated by Ca

Indexed as

Adenosine TriphosphateCalciumIon Channel GatingRyanodine Receptor Calcium Release ChannelAnimalsHumansAdenosine TriphosphateCalciumRyanodine Receptor Calcium Release ChannelRYR1 protein, human

Identifiers

PMID39994184
PMCPMC11850639

What OpenQuestion holds

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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.