Evidence map›Paper›PMID 30867421›Full record

ArticleNature communications2019

Calcium-activated 14-3-3 proteins as a molecular switch in salt stress tolerance.

Zhijia Yang, Chongwu Wang, Yuan Xue, Xiao Liu, She Chen, ChunPeng Song, Yongqing Yang, Yan Guo

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
10.4field-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

118 citing papers in PubMed, 278 citations in OpenAlex.

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  12. LjCIPK1: a CBL-interacting protein kinase fromFrontiers in plant science · 2026
    Article
  13. Article
  14. Article
  15. Review
  16. The Ionic and Metabolic Response Mechanisms ofPlants (Basel, Switzerland) · 2025
    Article
  17. Review
  18. Review
  19. CaNature communications · 2025
    Article
  20. Article

58 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 3 institutions in 1 country.

Zhijia YangState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China.
Chongwu WangState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China.ORCID http://orcid.org/0000-0001-9836-3464
Yuan XueState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China.
Xiao LiuState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China.
She ChenNational Institute of Biological Sciences, Beijing, 7 Science Park Road, Zhongguancun Life Science Park, 102206, Beijing, China.
ChunPeng SongCollaborative Innovation Center of Crop Stress Biology, Henan Province, Institute of Plant Stress Biology, Henan University, 475001, Kaifeng, China.ORCID http://orcid.org/0000-0001-8774-4309
Yongqing YangState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China. yangyongqing@cau.edu.cn.
Yan GuoState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China. guoyan@cau.edu.cn.ORCID http://orcid.org/0000-0002-6955-8008
China Agricultural University · CNHenan University · CNNational Institute of Biological Sciences, Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium is a universal secondary messenger that triggers many cellular responses. However, it is unclear how a calcium signal is coordinately decoded by different calcium sensors, which in turn regulate downstream targets to fulfill a specific physiological function. Here we show that SOS2-LIKE PROTEIN KINASE5 (PKS5) can negatively regulate the Salt-Overly-Sensitive signaling pathway in Arabidopsis. PKS5 can interact with and phosphorylate SOS2 at Ser

Indexed as

14-3-3 ProteinsArabidopsisArabidopsis ProteinsCalciumCalcium-Binding ProteinsPhosphorylationPlants, Genetically ModifiedProtein BindingProtein Serine-Threonine KinasesProton-Translocating ATPasesSalt StressSalt ToleranceSignal TransductionSodiumSodium-Hydrogen Exchangers14-3-3 ProteinsArabidopsis ProteinsCalciumCalcium-Binding ProteinsCBL10 protein, ArabidopsisProtein Serine-Threonine KinasesProton-Translocating ATPasesSIP4 protein, ArabidopsisSodiumSodium-Hydrogen ExchangersSOS2 protein, ArabidopsisSOS3 protein, Arabidopsis

Identifiers

PMID30867421
PMCPMC6416337
OpenAlexW2922059199

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.