Evidence map›Paper›PMID 27869186›Full record

ArticleScientific reports2016

Regulation of Anticancer Styrylpyrone Biosynthesis in the Medicinal Mushroom Inonotus obliquus Requires Thioredoxin Mediated Transnitrosylation of S-nitrosoglutathione Reductase.

Yanxia Zhao, Meihong He, Jianing Ding, Qi Xi, Gary J Loake, Weifa Zheng

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
1.5field-weighted citation impact, top 16% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Metabolic modulation of TCA cycle bySynthetic and systems biotechnology · 2026
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  5. Review
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  7. RNA-Seq de Novo Assembly and Differential Transcriptome Analysis of Chaga (International journal of molecular sciences · 2019
    Article
  8. Article
  9. Review
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 2 countries.

Yanxia ZhaoLaboratory for Biotechnology of Medicinal Plants, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China.
Meihong HeLaboratory for Biotechnology of Medicinal Plants, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China.
Jianing DingLaboratory for Biotechnology of Medicinal Plants, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China.
Qi XiLaboratory for Biotechnology of Medicinal Plants, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China.
Gary J LoakeInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Weifa ZhengLaboratory for Biotechnology of Medicinal Plants, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China.
Jiangsu Normal University · CNUniversity of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D011809/1Biotechnology and Biological Sciences Research Council BB/H000984/1
6 · The paper itself

Abstract

The medicinal macrofungus Inonotus obliquus widely utilized as folk medicine in Russia and Baltic countries is a source of phenylpropanoid-derived styrylpyrone polyphenols that can inhibit tumor proliferation. Insights into the regulatory machinery that controls I. obliquus styrylpyrone polyphenol biosynthesis will enable strategies to increase the production of these molecules. Here we show that Thioredoxin (Trx) mediated transnitrosylation of S-nitrosoglutathione reductase (GSNOR) underpins the regulation of styrylpyrone production, driven by nitric oxide (NO) synthesis triggered by P. morii coculture. NO accumulation results in the S-nitrosylation of PAL and 4CL required for the synthesis of precursor phenylpropanoids and styrylpyrone synthase (SPS), integral to the production of styrylpyrone, inhibiting their activities. These enzymes are targeted for denitrosylation by Trx proteins, which restore their activity. Further, this Trx S-nitrosothiol (SNO) reductase activity was potentiated following S-nitrosylation of Trx proteins at a non-catalytic cysteine (Cys) residue. Intriguingly, this process was counterbalanced by Trx denitrosylation, mediated by Trx-dependent transnitrosylation of GSNOR. Thus, unprecedented interplay between Trx and GSNOR oxidoreductases regulates the biosynthesis of styrylpyrone polyphenols in I. obliquus.

Indexed as

AgaricalesAldehyde OxidoreductasesAntineoplastic AgentsBiocatalysisChromatography, LiquidCoculture TechniquesModels, BiologicalNitrosationNitrosative StressOxidation-ReductionPolyphenolsProtein BindingPyronesTandem Mass SpectrometryThioredoxinsAldehyde OxidoreductasesAntineoplastic Agentsformaldehyde dehydrogenase, glutathione-independentPolyphenolsPyronesThioredoxins

Identifiers

PMID27869186
PMCPMC5116637
OpenAlexW2551339155

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Textmetadata
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.