Evidence map›Paper›PMID 30467384›Full record

ArticleScientific reports2018

Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis.

Laure Aymé, Simon Arragain, Michel Canonge, Sébastien Baud, Nadia Touati, Ornella Bimai, Franjo Jagic, Christelle Louis-Mondésir, Pierre Briozzo, Marc Fontecave 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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

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  10. Genome-Wide Identification, Classification, and Expression Analyses of theInternational journal of molecular sciences · 2023
    Article
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  14. The pathway for coenzyme M biosynthesis in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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 1 institution in 1 country.

Laure AyméInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France.
Simon ArragainLaboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Université Paris 6, 11 Place Marcelin Berthelot, 75231, Paris, CEDEX 05, France.
Michel CanongeInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France.
Sébastien BaudInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France.
Nadia TouatiChimie ParisTech, PSL Research University, CNRS, Institut de Recherche de Chimie Paris (IRCP), F-75005, Paris, France.
Ornella BimaiLaboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Université Paris 6, 11 Place Marcelin Berthelot, 75231, Paris, CEDEX 05, France.
Franjo JagicInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France.
Christelle Louis-MondésirInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France.
Pierre BriozzoInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France.
Marc FontecaveLaboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Université Paris 6, 11 Place Marcelin Berthelot, 75231, Paris, CEDEX 05, France. marc.fontecave@college-de-france.fr.
Thierry ChardotInstitut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France. thierry.chardot@inra.fr.ORCID http://orcid.org/0000-0001-6689-6151
Centre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche (French National Research Agency) Labex program DYNAMO, ANR-11-LABX-0011Agence Nationale de la Recherche (French National Research Agency) LABX-0040-SPSAgence Nationale de la Recherche (French National Research Agency) LABX-040
6 · The paper itself

Abstract

Acyl-CoA:diacylglycerol acyltransferases 3 (DGAT3) are described as plant cytosolic enzymes synthesizing triacylglycerol. Their protein sequences exhibit a thioredoxin-like ferredoxin domain typical of a class of ferredoxins harboring a [2Fe-2S] cluster. The Arabidopsis thaliana DGAT3 (AtDGAT3; At1g48300) protein is detected in germinating seeds. The recombinant purified protein produced from Escherichia coli, although very unstable, exhibits DGAT activity in vitro. A shorter protein version devoid of its N-terminal putative chloroplast transit peptide, Δ46AtDGAT3, was more stable in vitro, allowing biochemical and spectroscopic characterization. The results obtained demonstrate the presence of a [2Fe-2S] cluster in the protein. To date, AtDGAT3 is the first metalloprotein described as a DGAT.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsDiacylglycerol O-AcyltransferaseEscherichia coliGerminationIron-Sulfur ProteinsProtein DomainsProtein StabilityRecombinant ProteinsSeedsThioredoxinsArabidopsis ProteinsAT1G48300 protein, ArabidopsisDiacylglycerol O-AcyltransferaseIron-Sulfur ProteinsRecombinant ProteinsThioredoxins

Identifiers

PMID30467384
PMCPMC6250708
OpenAlexW2901597177

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.