Evidence map›Paper›PMID 34135385›Full record

ArticleScientific reports2021

Biochemical consequences of two clinically relevant ND-gene mutations in Escherichia coli respiratory complex I.

Franziska Nuber, Johannes Schimpf, Jean-Paul di Rago, Déborah Tribouillard-Tanvier, Vincent Procaccio, Marie-Laure Martin-Negrier, Aurélien Trimouille, Olivier Biner, Christoph von Ballmoos, Thorsten Friedrich

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. A fixed mutation in the respiratory complex I impairs mitochondrial bioenergetics in the endangered Apennine brown bear.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. HScientific reports · 2023
    Article
  5. Respiratory complex I with charge symmetry in the membrane arm pumps protons.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. 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

10 authors at 6 institutions in 4 countries.

Franziska NuberInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Johannes SchimpfInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Jean-Paul di RagoIBGC, CNRS UMR5095, Bordeaux University, Bordeaux, France.
Déborah Tribouillard-TanvierIBGC, CNRS UMR5095, Bordeaux University, Bordeaux, France.
Vincent ProcaccioMitoLab, UMR CNRS 6015-INSERM U1083, Université d'Angers, Angers, France.
Marie-Laure Martin-NegrierCHU de Bordeaux, 33000, Bordeaux, France. marie-laure.martin-negrier@u-bordeaux.fr.
Aurélien TrimouilleCHU de Bordeaux, 33000, Bordeaux, France.
Olivier BinerDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Christoph von BallmoosDepartment of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
Thorsten FriedrichInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany. Friedrich@bio.chemie.uni-freiburg.de.
University of Freiburg · DECentre National de la Recherche Scientifique · FRUniversity of Bern · CHCentre Hospitalier Universitaire de Bordeaux · FRUniversité d'Angers · FRUniversité de Bordeaux · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

nadhubiquinone oxidoreductase (respiratory complex I) plays a major role in energy metabolism by coupling electron transfer from NADH to quinone with proton translocation across the membrane. Complex I deficiencies were found to be the most common source of human mitochondrial dysfunction that manifest in a wide variety of neurodegenerative diseases. Seven subunits of human complex I are encoded by mitochondrial DNA (mtDNA) that carry an unexpectedly large number of mutations discovered in mitochondria from patients' tissues. However, whether or how these genetic aberrations affect complex I at a molecular level is unknown. Here, we used Escherichia coli as a model system to biochemically characterize two mutations that were found in mtDNA of patients. The V253A

Indexed as

MutationAdultBenzoquinonesElectron Transport Complex IEscherichia coliHumansInfant, NewbornMitochondrial ProteinsModels, MolecularNADH DehydrogenaseOperonPlasmidsBenzoquinonesElectron Transport Complex IMitochondrial ProteinsMT-ND5 protein, humanNADH DehydrogenaseNADH dehydrogenase IINADH dehydrogenase subunit 1, humanquinone

Identifiers

PMID34135385
PMCPMC8209014
OpenAlexW3170776059

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.