Evidence map›Paper›PMID 29946152›Full record

ArticleScientific reports2018

The atypical subunit composition of respiratory complexes I and IV is associated with original extra structural domains in Euglena gracilis.

H V Miranda-Astudillo, K N S Yadav, L Colina-Tenorio, F Bouillenne, H Degand, P Morsomme, E J Boekema, P Cardol

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Euglena gracilis Subcellular Fractionation.Methods in molecular biology (Clifton, N.J.) · 2026
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  3. Review
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  10. Genes · 2021
    Article
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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

8 authors at 4 institutions in 3 countries.

H V Miranda-AstudilloLaboratoire de Génétique et Physiologie des microalgues, InBioS/Phytosystems, Institut de Botanique, Université de Liège, Liege, Belgium.
K N S YadavDepartment of Electron Microscopy, Groningen Biological Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
L Colina-TenorioDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico, Mexico.
F BouillenneInBioS/Center for Protein Engineering, Université de Liège, Liege, Belgium.
H DegandInstitut des Sciences de la Vie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
P MorsommeInstitut des Sciences de la Vie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
E J BoekemaDepartment of Electron Microscopy, Groningen Biological Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
P CardolLaboratoire de Génétique et Physiologie des microalgues, InBioS/Phytosystems, Institut de Botanique, Université de Liège, Liege, Belgium. pierre.cardol@uliege.be.ORCID 0000-0001-9799-0546
University of Liège · BEUCLouvain · BEUniversity of Groningen · NLUniversidad Nacional Autónoma de México · MX

Funding

EC | European Research Council (ERC) 682580Fonds De La Recherche Scientifique - FNRS (Belgian National Fund for Scientific Research) CDR J.0079Fonds De La Recherche Scientifique - FNRS (Belgian National Fund for Scientific Research) FRFC 2.4597
6 · The paper itself

Abstract

In mitochondrial oxidative phosphorylation, electron transfer from NADH or succinate to oxygen by a series of large protein complexes in the inner mitochondrial membrane (complexes I-IV) is coupled to the generation of an electrochemical proton gradient, the energy of which is utilized by complex V to generate ATP. In Euglena gracilis, a non-parasitic secondary green alga related to trypanosomes, these respiratory complexes totalize more than 40 Euglenozoa-specific subunits along with about 50 classical subunits described in other eukaryotes. In the present study the Euglena proton-pumping complexes I, III, and IV were purified from isolated mitochondria by a two-steps liquid chromatography approach. Their atypical subunit composition was further resolved and confirmed using a three-steps PAGE analysis coupled to mass spectrometry identification of peptides. The purified complexes were also observed by electron microscopy followed by single-particle analysis. Even if the overall structures of the three oxidases are similar to the structure of canonical enzymes (e.g. from mammals), additional atypical domains were observed in complexes I and IV: an extra domain located at the tip of the peripheral arm of complex I and a "helmet-like" domain on the top of the cytochrome c binding region in complex IV.

Indexed as

AnimalsElectron TransportElectron Transport Complex IElectron Transport Complex IVEuglena gracilisMitochondriaMitochondrial MembranesOxidative PhosphorylationElectron Transport Complex IElectron Transport Complex IV

Identifiers

PMID29946152
PMCPMC6018760
OpenAlexW2809193439

What OpenQuestion holds

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LicenceCC BY
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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.