Evidence map›Paper›PMID 25742495›Full record

ArticlePloS one2015

Molecular and Biochemical Analysis of Chalcone Synthase from Freesia hybrid in flavonoid biosynthetic pathway.

Wei Sun, Xiangyu Meng, Lingjie Liang, Wangshu Jiang, Yafei Huang, Jing He, Haiyan Hu, Jonas Almqvist, Xiang Gao, Li Wang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

73 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
  2. Identification and Expression Profile of the Chalcone Synthase (International journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Influence of Secondary Metabolites According to Maturation of Perilla (International journal of molecular sciences · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Chalcone-Synthase-EncodingMolecules (Basel, Switzerland) · 2024
    Article
  19. Article
  20. Article

13 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

10 authors at 2 institutions in 2 countries.

Wei SunInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Xiangyu MengInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Lingjie LiangInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Wangshu JiangDepartment of Cell and Molecular Biology, Uppsala University, Uppsala Biomedical Center, Uppsala, 596, S-75124, Sweden.
Yafei HuangDepartment of Cell and Molecular Biology, Uppsala University, Uppsala Biomedical Center, Uppsala, 596, S-75124, Sweden.
Jing HeInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Haiyan HuInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Jonas AlmqvistDepartment of Cell and Molecular Biology, Uppsala University, Uppsala Biomedical Center, Uppsala, 596, S-75124, Sweden.
Xiang GaoInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Li WangInstitute of Genetics and Cytology, Northeast Normal University, Changchun, China.
Northeast Normal University · CNUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chalcone synthase (CHS) catalyzes the first committed step in the flavonoid biosynthetic pathway. In this study, the cDNA (FhCHS1) encoding CHS from Freesia hybrida was successfully isolated and analyzed. Multiple sequence alignments showed that both the conserved CHS active site residues and CHS signature sequence were found in the deduced amino acid sequence of FhCHS1. Meanwhile, crystallographic analysis revealed that protein structure of FhCHS1 is highly similar to that of alfalfa CHS2, and the biochemical analysis results indicated that it has an enzymatic role in naringenin biosynthesis. Moreover, quantitative real-time PCR was performed to detect the transcript levels of FhCHS1 in flowers and different tissues, and patterns of FhCHS1 expression in flowers showed significant correlation to the accumulation patterns of anthocyanin during flower development. To further characterize the functionality of FhCHS1, its ectopic expression in Arabidopsis thaliana tt4 mutants and Petunia hybrida was performed. The results showed that overexpression of FhCHS1 in tt4 mutants fully restored the pigmentation phenotype of the seed coats, cotyledons and hypocotyls, while transgenic petunia expressing FhCHS1 showed flower color alteration from white to pink. In summary, these results suggest that FhCHS1 plays an essential role in the biosynthesis of flavonoid in Freesia hybrida and may be used to modify the components of flavonoids in other plants.

Indexed as

AcyltransferasesBiosynthetic PathwaysCatalytic DomainCloning, MolecularCrystallographyFlavonoidsFlowersIridaceaeModels, MolecularMutationPlant ProteinsProtein Structure, TertiaryAcyltransferasesflavanone synthetaseFlavonoidsPlant Proteins

Identifiers

PMID25742495
PMCPMC4351062
OpenAlexW2113373428

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LicenceCC BY
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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.