Evidence map›Paper›PMID 30498218›Full record

ArticleNature communications2018

Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2.

Xin Liu, Jiawei Wang, Linfeng Sun

Abstract 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 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing 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

91 citing papers in PubMed.

  1. TheInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Calcium-activated chloride channel TMEM16A opens via pi-helical transition in transmembrane segment 4.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Review
  17. The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025
    Review
  18. Article
  19. Review
  20. Review

31 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

3 authors.

Xin LiuHefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 230027, Hefei, China.
Jiawei WangState Key Laboratory of Membrane Biology, Beijing Advanced Innovation Centre for Structural Biology, School of Life Sciences, Tsinghua University, 100084, Beijing, China. jwwang@mail.tsinghua.edu.cn.
Linfeng SunHefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 230027, Hefei, China. sunlf17@ustc.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade initiated by cytosolic calcium concentration elevation. Members of the OSCA family in Arabidopsis thaliana, identified as the hyperosmolality-gated calcium-permeable channels, have been suggested to play a key role during the initial phase of hyperosmotic stress response. Here, we report the atomic structure of Arabidopsis OSCA1.2 determined by single-particle cryo-electron microscopy. It contains 11 transmembrane helices and forms a homodimer. It is in an inactivated state, and the pore-lining residues are clearly identified. Its cytosolic domain contains a RNA recognition motif and two unique long helices. The linker between these two helices forms an anchor in the lipid bilayer and may be essential to osmosensing. The structure of AtOSCA1.2 serves as a platform for the study of the mechanism underlying osmotic stress responses and mechanosensing.

Indexed as

ArabidopsisArabidopsis ProteinsCryoelectron MicroscopyLipid BilayersOsmotic PressureProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryArabidopsis ProteinsLipid Bilayers

Identifiers

PMID30498218
PMCPMC6265326

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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.