Evidence map›Paper›PMID 24743650›Full record

ArticlePloS one2014

Identification and characterization of ABA receptors in Oryza sativa.

Yuan He, Qi Hao, Wenqi Li, Chuangye Yan, Nieng Yan, Ping Yin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. 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
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

61 citing papers in PubMed, 155 citations in OpenAlex.

  1. Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Overexpression of the PotatoInternational journal of molecular sciences · 2024
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  16. International journal of molecular sciences · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Article

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

6 authors at 2 institutions in 1 country.

Yuan HeState Key Laboratory of Bio-membrane and Membrane Biotechnology, Beijing, China; Center for Structural Biology, School of Medicine, Beijing, China.
Qi HaoState Key Laboratory of Bio-membrane and Membrane Biotechnology, Beijing, China; Center for Structural Biology, School of Medicine, Beijing, China.
Wenqi LiState Key Laboratory of Bio-membrane and Membrane Biotechnology, Beijing, China; Center for Structural Biology, School of Medicine, Beijing, China.
Chuangye YanState Key Laboratory of Bio-membrane and Membrane Biotechnology, Beijing, China; School of Life Sciences, Tsinghua University, Beijing, China.
Nieng YanState Key Laboratory of Bio-membrane and Membrane Biotechnology, Beijing, China; Center for Structural Biology, School of Medicine, Beijing, China.
Ping YinNational Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Wuhan, China; College of Life Sciences and Technology, Huazhong Agricultural University, Wuhan, China.
Huazhong Agricultural University · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abscisic acid (ABA) is an essential phytohormone that regulates plant stress responses. ABA receptors in Arabidopsis thaliana (AtPYLs) have been extensively investigated by structural, biochemical, and in vivo studies. In contrast, relatively little is known about the ABA signal transduction cascade in rice. Besides, the diversities of AtPYLs manifest that the information accumulated in Arabidopsis cannot be simply adapted to rice. Thus, studies on rice ABA receptors are compulsory. By taking a bioinformatic approach, we identified twelve ABA receptor orthologs in Oryza sativa (japonica cultivar-group) (OsPYLs), named OsPYL1-12. We have successfully expressed and purified OsPYL1-3, 6 and 10-12 to homogeneity, tested the inhibitory effects on PP2C in Oryza sativa (OsPP2C), and measured their oligomerization states. OsPYL1-3 mainly exhibit as dimers and require ABA to inhibit PP2C's activity. On the contrary, OsPYL6 retains in the monomer-dimer equilibrium state and OsPYL10-11 largely exist as monomers, and they all display an ABA-independent phosphatase inhibition manner. Interestingly, although OsPYL12 seems to be a dimer, it abrogates the phosphatase activity of PP2Cs in the absence of ABA. Toward a further understanding of OsPYLs on the ABA binding and PP2C inhibition, we determined the crystal structure of ABA-OsPYL2-OsPP2C06 complex. The bioinformatic, biochemical and structural analysis of ABA receptors in rice provide important foundations for designing rational ABA-analogues and breeding the stress-resistant rice for commercial agriculture.

Indexed as

OryzaPlant ProteinsReceptors, Cell SurfaceAbscisic AcidPhosphoprotein PhosphatasesProtein MultimerizationProtein Phosphatase 2CSignal TransductionAbscisic AcidPhosphoprotein PhosphatasesPlant ProteinsProtein Phosphatase 2CReceptors, Cell Surface

Identifiers

PMID24743650
PMCPMC3990689
OpenAlexW2050981405

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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.