Evidence map›Paper›PMID 29021545›Full record

ArticleNature communications2017

The metabolic enzyme fructose-1,6-bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella.

Jason Ziveri, Fabiola Tros, Ida Chiara Guerrera, Cerina Chhuon, Mathilde Audry, Marion Dupuis, Monique Barel, Sarantis Korniotis, Simon Fillatreau, Lara Gales and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 104 citations in OpenAlex.

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  12. Cloning and Characterization of Fructose-1,6-Bisphosphate Aldolase fromInternational journal of molecular sciences · 2022
    Article
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  16. Proteomic analysis response of rice (Frontiers in plant science · 2022
    Article
  17. Frontiers in immunology · 2022
    Review
  18. Article
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  20. 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

12 authors at 2 institutions in 2 countries.

Jason ZiveriUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Fabiola TrosUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Ida Chiara GuerreraUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Cerina ChhuonUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Mathilde AudryUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Marion DupuisUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Monique BarelUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Sarantis KorniotisUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Simon FillatreauUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France.
Lara GalesMetatoul Platform, LISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, 31077, France.
Edern CahoreauMetatoul Platform, LISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, 31077, France.
Alain CharbitUniversité Paris Descartes, Sorbonne Paris Cité, Bâtiment Leriche, Paris, 75993, France. alain.charbit@inserm.fr.ORCID http://orcid.org/0000-0001-5243-4861
Délégation Paris 5 · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme fructose-bisphosphate aldolase occupies a central position in glycolysis and gluconeogenesis pathways. Beyond its housekeeping role in metabolism, fructose-bisphosphate aldolase has been involved in additional functions and is considered as a potential target for drug development against pathogenic bacteria. Here, we address the role of fructose-bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, we unravel a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively. We propose a model in which fructose-bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response.The enzyme fructose-bisphosphate aldolase (FBA) plays central roles in glycolysis and gluconeogenesis. Here, Ziveri et al. show that FBA of the pathogen Francisella novicida acts, in addition, as a transcriptional regulator and is important for bacterial multiplication in macrophages.

Indexed as

Gene Expression Regulation, BacterialAnimalsFemaleFrancisella tularensisFructose-Bisphosphate AldolaseGluconeogenesisGlucoseMacrophagesMetabolomicsMice, Inbred BALB COxidative StressFructose-Bisphosphate AldolaseGlucose

Identifiers

PMID29021545
PMCPMC5636795
OpenAlexW2763729736

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.