Evidence map›Paper›PMID 26049045›Full record

ArticleBiochemical pharmacology2015

The phenotype of a knockout mouse identifies flavin-containing monooxygenase 5 (FMO5) as a regulator of metabolic ageing.

Sandra G Gonzalez Malagon, Anna N Melidoni, Diana Hernandez, Bilal A Omar, Lyndsey Houseman, Sunil Veeravalli, Flora Scott, Dorsa Varshavi, Jeremy Everett, Yugo Tsuchiya and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Biochemical pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Phenotypic and metabonomics studies of FMOs in C. elegans and their roles in lifespan extension.Metabolomics : Official journal of the Metabolomic Society · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Flavin-containing monooxygenase (FMO): Beyond xenobiotics.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Flavin-containing monooxygenases: new structures from old proteins.Nature structural & molecular biology · 2020
    Article
  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

13 authors at 4 institutions in 1 country.

Sandra G Gonzalez MalagonInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Anna N MelidoniSchool of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.
Diana HernandezInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Bilal A OmarSchool of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.
Lyndsey HousemanInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Sunil VeeravalliInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Flora ScottInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Dorsa VarshaviMedway Metabonomics Research Group, University of Greenwich, Chatham Maritime, Kent ME4 4TB, UK.
Jeremy EverettMedway Metabonomics Research Group, University of Greenwich, Chatham Maritime, Kent ME4 4TB, UK.
Yugo TsuchiyaInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
John F TimmsWomen's Cancer, Institute for Women's Health, University College London, London WC1E 6BT, UK.
Ian R PhillipsInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK; School of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.
Elizabeth A ShephardInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK. Electronic address: e.shephard@ucl.ac.uk.
Institute of Structural and Molecular Biology · GBQueen Mary University of London · GBUniversity of Greenwich · GBUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report the production and metabolic phenotype of a mouse line in which the Fmo5 gene is disrupted. In comparison with wild-type (WT) mice, Fmo5(-/-) mice exhibit a lean phenotype, which is age-related, becoming apparent after 20 weeks of age. Despite greater food intake, Fmo5(-/-) mice weigh less, store less fat in white adipose tissue (WAT), have lower plasma glucose and cholesterol concentrations and enhanced whole-body energy expenditure, due mostly to increased resting energy expenditure, with no increase in physical activity. An increase in respiratory exchange ratio during the dark phase, the period in which the mice are active, indicates a switch from fat to carbohydrate oxidation. In comparison with WT mice, the rate of fatty acid oxidation in Fmo5(-/-) mice is higher in WAT, which would contribute to depletion of lipid stores in this tissue, and lower in skeletal muscle. Five proteins were down regulated in the liver of Fmo5(-/-) mice: aldolase B, ketohexokinase and cytosolic glycerol 3-phosphate dehydrogenase (GPD1) are involved in glucose or fructose metabolism and GPD1 also in production of glycerol 3-phosphate, a precursor of triglyceride biosynthesis; HMG-CoA synthase 1 is involved in cholesterol biosynthesis; and malic enzyme 1 catalyzes the oxidative decarboxylation of malate to pyruvate, in the process producing NADPH for use in lipid and cholesterol biosynthesis. Down regulation of these proteins provides a potential explanation for the reduced fat deposits and lower plasma cholesterol characteristic of Fmo5(-/-) mice. Our results indicate that disruption of the Fmo5 gene slows metabolic ageing via pleiotropic effects.

Indexed as

Founder EffectGene Expression RegulationAdipose Tissue, WhiteAgingAnimalsBlood GlucoseBody WeightCholesterolEnergy MetabolismFructokinasesFructose-Bisphosphate AldolaseGenotypeGlycerol-3-Phosphate Dehydrogenase (NAD+)Hydroxymethylglutaryl-CoA SynthaseLipid MetabolismLiverBlood GlucoseCholesteroldimethylaniline monooxygenase (N-oxide forming)FructokinasesFructose-Bisphosphate AldolaseGlycerol-3-Phosphate Dehydrogenase (NAD+)Hydroxymethylglutaryl-CoA SynthaseketohexokinaseMalate DehydrogenaseOxygenasesBody weightCholesterolGlucoseMalic enzyme 1White adipose tissue

Identifiers

PMID26049045
PMCPMC4509511
OpenAlexW2086461147

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.