Evidence map›Paper›PMID 29132502›Full record

ArticleeLife2017

Transcriptomic and proteomic landscape of mitochondrial dysfunction reveals secondary coenzyme Q deficiency in mammals.

Inge Kühl, Maria Miranda, Ilian Atanassov, Irina Kuznetsova, Yvonne Hinze, Arnaud Mourier, Aleksandra Filipovska, Nils-Göran Larsson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 273 citations in OpenAlex.

  1. The efficacy of coenzyme QJournal of cellular and molecular medicine · 2022
    Pooled it
  2. The mitochondrial chaperone HSPD1 folds MTHFD2 independently of its co-chaperone HSPE1.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Article
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  10. Perturbation of mitochondrial CaStress biology · 2026
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80 more citing papers are in PubMed but not listed here.

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

8 authors at 5 institutions in 4 countries.

Inge Kühl *Department of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Cologne, Germany.ORCID http://orcid.org/0000-0003-4797-0859
Maria Miranda *Department of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Cologne, Germany.ORCID http://orcid.org/0000-0002-0817-553X
Ilian AtanassovProteomics Core Facility, Max Planck Institute for Biology of Ageing, Cologne, Germany.ORCID https://orcid.org/0000-0001-8259-2545
Irina KuznetsovaHarry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia.
Yvonne HinzeProteomics Core Facility, Max Planck Institute for Biology of Ageing, Cologne, Germany.
Arnaud MourierThe Centre National de la Recherche Scientifique, Institut de Biochimie et Génétique Cellulaires, Université de Bordeaux, Bordeaux, France.
Aleksandra FilipovskaHarry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia.ORCID http://orcid.org/0000-0002-6998-8403
Nils-Göran LarssonDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Cologne, Germany.ORCID http://orcid.org/0000-0001-5100-996X
Max Planck Institute for Biology of Ageing · DEThe University of Western Australia · AUKarolinska Institutet · SEUniversité de Bordeaux · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysfunction of the oxidative phosphorylation (OXPHOS) system is a major cause of human disease and the cellular consequences are highly complex. Here, we present comparative analyses of mitochondrial proteomes, cellular transcriptomes and targeted metabolomics of five knockout mouse strains deficient in essential factors required for mitochondrial DNA gene expression, leading to OXPHOS dysfunction. Moreover, we describe sequential protein changes during post-natal development and progressive OXPHOS dysfunction in time course analyses in control mice and a middle lifespan knockout, respectively. Very unexpectedly, we identify a new response pathway to OXPHOS dysfunction in which the intra-mitochondrial synthesis of coenzyme Q (ubiquinone, Q) and Q levels are profoundly decreased, pointing towards novel possibilities for therapy. Our extensive omics analyses provide a high-quality resource of altered gene expression patterns under severe OXPHOS deficiency comparing several mouse models, that will deepen our understanding, open avenues for research and provide an important reference for diagnosis and treatment.

Indexed as

Gene Expression ProfilingMetabolomeAnimalsAtaxiaMice, KnockoutMitochondriaMitochondrial DiseasesMuscle WeaknessProteomeUbiquinoneProteomeUbiquinonebiochemistrycell biologyCellular transcriptomeCoenzyme Q biosynthesisMitochondrial gene expressionMitoproteomemouseOne-carbon pathwayOXPHOS dysfunction

Identifiers

PMID29132502
PMCPMC5703644
OpenAlexW2769589482

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.