Evidence map›Paper›PMID 41159738›Full record

ArticlemBio2025

The essential role of 2,4-dienoyl-CoA reductase for the degradation of complex fatty acid mixtures.

Veronica Schiaffi, Viola Pavoncello, Bastien Prost, Audrey Solgadi, Frédéric Barras, Emmanuelle Bouveret

Abstract read
In one paragraph

Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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.

Veronica Schiaffi *SAMe Unit, Department of Microbiology, UMR CNRS 6047, Université Paris-Cité, Institut Pasteur, Paris, France.
Viola Pavoncello *SAMe Unit, Department of Microbiology, UMR CNRS 6047, Université Paris-Cité, Institut Pasteur, Paris, France.
Bastien ProstUMS-IPSIT-Platform SAMM, Université Paris-Saclay, Orsay, France.
Audrey SolgadiUMS-IPSIT-Platform SAMM, Université Paris-Saclay, Orsay, France.
Frédéric BarrasSAMe Unit, Department of Microbiology, UMR CNRS 6047, Université Paris-Cité, Institut Pasteur, Paris, France.ORCID 0000-0003-3458-2574
Emmanuelle BouveretSAMe Unit, Department of Microbiology, UMR CNRS 6047, Université Paris-Cité, Institut Pasteur, Paris, France.ORCID 0000-0001-5511-6375

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fatty acids (FAs) can be used as a carbon and energy source by most bacteria. FAs are diverse and show variations in aliphatic chain length, degree and kind of branching, and number of double bonds. After activation by a thioester link to coenzyme A (CoA), FAs are degraded by the β-oxidation machinery. The core β-oxidation enzymes can degrade most FAs, except those that bear an unsaturation at even-numbered carbons. Such FAs include the essential arachidonic and linoleic FAs of the mammalian diet. We studied the role of the 2,4-dienoyl-CoA reductase FadH in

Indexed as

Escherichia coliFatty AcidsLinoleic AcidOxidation-ReductionOxidoreductases Acting on CH-CH Group Donors2,4-dienoyl-CoA reductaseFatty AcidsLinoleic AcidOxidoreductases Acting on CH-CH Group Donors2,4‑dienoyl‑CoA reductase[4Fe-4S] clusterDECREscherichia coliFadHfatty acid degradationlinoleic acid

Identifiers

PMID41159738
PMCPMC12691678

What OpenQuestion holds

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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.