Evidence map›Paper›PMID 29855494›Full record

ArticleScientific reports2018

Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor.

Mathieu Schwartz, Thomas Perrot, Emmanuel Aubert, Stéphane Dumarçay, Frédérique Favier, Philippe Gérardin, Mélanie Morel-Rouhier, Guillermo Mulliert, Fanny Saiag, Claude Didierjean and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.7field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  6. Qualitative metabolomics-based characterization of a phenolic UDP-xylosyltransferase with a broad substrate spectrum fromProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Review
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  9. Article
  10. Article
  11. Review
  12. Fungal bioassays for environmental monitoring.Frontiers in bioengineering and biotechnology · 2022
    Review
  13. Article
  14. Article
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  16. Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  17. Article
  18. Article
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

11 authors at 3 institutions in 1 country.

Mathieu SchwartzUniversité de Lorraine, CNRS, CRM2, Nancy, France.
Thomas PerrotUniversité de Lorraine, INRA, IAM, Nancy, France.
Emmanuel AubertUniversité de Lorraine, CNRS, CRM2, Nancy, France.
Stéphane DumarçayUniversité de Lorraine, LERMAB, Nancy, France.
Frédérique FavierUniversité de Lorraine, CNRS, CRM2, Nancy, France.
Philippe GérardinUniversité de Lorraine, LERMAB, Nancy, France.
Mélanie Morel-RouhierUniversité de Lorraine, INRA, IAM, Nancy, France.
Guillermo MulliertUniversité de Lorraine, CNRS, CRM2, Nancy, France.
Fanny SaiagUniversité de Lorraine, INRA, IAM, Nancy, France.
Claude DidierjeanUniversité de Lorraine, CNRS, CRM2, Nancy, France. claude.didierjean@univ-lorraine.fr.
Eric GelhayeUniversité de Lorraine, INRA, IAM, Nancy, France. eric.gelhaye@univ-lorraine.fr.ORCID 0000-0002-0699-9113
Centre National de la Recherche Scientifique · FRInteractions Arbres-Microorganismes · FRLaboratoire d'Etude et de Recherche sur le Matériau Bois · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Wood decay fungi have complex detoxification systems that enable them to cope with secondary metabolites produced by plants. Although the number of genes encoding for glutathione transferases is especially expanded in lignolytic fungi, little is known about their target molecules. In this study, by combining biochemical, enzymatic and structural approaches, interactions between polyphenols and six glutathione transferases from the white-rot fungus Trametes versicolor have been demonstrated. Two isoforms, named TvGSTO3S and TvGSTO6S have been deeply studied at the structural level. Each isoform shows two distinct ligand-binding sites, a narrow L-site at the dimer interface and a peculiar deep hydrophobic H-site. In TvGSTO3S, the latter appears optimized for aromatic ligand binding such as hydroxybenzophenones. Affinity crystallography revealed that this H-site retains the flavonoid dihydrowogonin from a partially purified wild-cherry extract. Besides, TvGSTO6S binds two molecules of the flavonoid naringenin in the L-site. These data suggest that TvGSTO isoforms could interact with plant polyphenols released during wood degradation.

Indexed as

Metabolic Detoxication, Phase IIAmino Acid SequenceBenzophenonesBinding SitesCrystallography, X-RayFlavonoidsFungal ProteinsGlutathione TransferaseIsoenzymesKineticsPolyphenolsProtein StabilityProtein Structure, TertiaryPrunusSequence AlignmentTemperatureBenzophenonesFlavonoidsFungal ProteinsGlutathione TransferaseIsoenzymesPolyphenols

Identifiers

PMID29855494
PMCPMC5981210
OpenAlexW2805541372

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.