Evidence map›Paper›PMID 38243131›Full record

ArticleNature metabolism2024

An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis.

Juan Cruz Herrero Martín, Beñat Salegi Ansa, Gerardo Álvarez-Rivera, Sonia Domínguez-Zorita, Pilar Rodríguez-Pombo, Belén Pérez, Enrique Calvo, Alberto Paradela, David G Miguez, Alejandro Cifuentes and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Nature metabolism, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 2 pooled it
9.4field-weighted citation impact, top 1% 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

34 citing papers in PubMed, 2 syntheses or guidelines pooled it, 40 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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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

12 authors at 5 institutions in 1 country.

Juan Cruz Herrero Martín *Departamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0002-2542-1536
Beñat Salegi Ansa *Departamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0001-5054-758X
Gerardo Álvarez-RiveraLaboratorio Foodomics, Instituto de Investigación en Ciencias de la Alimentación (CIAL), Consejo Superior de Investigaciones Científicas (CSIC)-Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0003-1657-8141
Sonia Domínguez-ZoritaDepartamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0001-5764-3531
Pilar Rodríguez-PomboDepartamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0001-9315-5906
Belén PérezDepartamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain.
Enrique CalvoProteomics Unit, Centro Nacional de Investigaciones Cardiovasculares (CNIC) Carlos III, Madrid, Spain.
Alberto ParadelaProteomics Unit, Centro Nacional de Biotecnología (CNB)-Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.ORCID http://orcid.org/0000-0001-6837-7056
David G MiguezInstituto Universitario de Biología Molecular (IUBM), Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0001-8065-1142
Alejandro CifuentesLaboratorio Foodomics, Instituto de Investigación en Ciencias de la Alimentación (CIAL), Consejo Superior de Investigaciones Científicas (CSIC)-Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0002-7464-0217
José M CuezvaDepartamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain.ORCID http://orcid.org/0000-0003-1118-248X
Laura FormentiniDepartamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CBMSO, UAM-CSIC), Universidad Autónoma de Madrid (UAM), Madrid, Spain. lformentini@cbm.csic.es.ORCID http://orcid.org/0000-0001-5641-821X
Instituto de Salud Carlos III · ESConsejo Superior de Investigaciones Científicas · ESCentro de Biología Molecular Severo Ochoa · ESSpanish National Centre for Cardiovascular Research · ESUniversidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coenzyme Q (Q) is a key lipid electron transporter, but several aspects of its biosynthesis and redox homeostasis remain undefined. Various flavoproteins reduce ubiquinone (oxidized form of Q) to ubiquinol (QH

Indexed as

Electron-Transferring FlavoproteinsOxidative PhosphorylationUbiquinoneAnimalsHomeostasisLipidsMiceMuscle, SkeletalElectron-Transferring FlavoproteinsLipidsUbiquinone

Identifiers

PMID38243131
PMCPMC10896730
OpenAlexW4391027820

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.