Evidence map›Paper›PMID 29704824›Full record

ArticleRedox biology2018

The mitochondrial oxidoreductase CHCHD4 is present in a semi-oxidized state in vivo.

Alican J Erdogan, Muna Ali, Markus Habich, Silja L Salscheider, Laura Schu, Carmelina Petrungaro, Luke W Thomas, Margaret Ashcroft, Lars I Leichert, Leticia Prates Roma and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

  1. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
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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

11 authors at 5 institutions in 2 countries.

Alican J ErdoganDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany.
Muna AliDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany; Department of Biology, Cellular Biochemistry, University of Kaiserslautern, Erwin-Schroedinger-Str. 13, 67663 Kaiserslautern, Germany.
Markus HabichDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany.
Silja L SalscheiderDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany.
Laura SchuDepartment of Biology, Cellular Biochemistry, University of Kaiserslautern, Erwin-Schroedinger-Str. 13, 67663 Kaiserslautern, Germany.
Carmelina PetrungaroDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany.
Luke W ThomasDepartment of Medicine, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Margaret AshcroftDepartment of Medicine, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Lars I LeichertInstitute for Biochemistry and Pathobiochemistry - Microbial Biochemistry, Ruhr-Universität Bochum, 44797 Bochum, Germany.
Leticia Prates RomaBiophysics Department, Center for Integrative Physiology and Molecular Medicine, Saarland University, 66421 Homburg, Saar, Germany.
Jan RiemerDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany. Electronic address: jan.riemer@uni-koeln.de.
University of Cologne · DEUniversity of Cambridge · GBRuhr University Bochum · DESaarland University · DEUniversity of Kaiserslautern · DE

Funding

Cancer Research UK 19442Medical Research Council MR/K002201/1Medical Research Council MR/K002201/2
6 · The paper itself

Abstract

Disulfide formation in the mitochondrial intermembrane space is an essential process catalyzed by a disulfide relay machinery. In mammalian cells, the key enzyme in this machinery is the oxidoreductase CHCHD4/Mia40. Here, we determined the in vivo CHCHD4 redox state, which is the major determinant of its cellular activity. We found that under basal conditions, endogenous CHCHD4 redox state in cultured cells and mouse tissues was predominantly oxidized, however, degrees of oxidation in different tissues varied from 70% to 90% oxidized. To test whether differences in the ratio between CHCHD4 and ALR might explain tissue-specific differences in the CHCHD4 redox state, we determined the molar ratio of both proteins in different mouse tissues. Surprisingly, ALR is superstoichiometric over CHCHD4 in most tissues. However, the levels of CHCHD4 and the ratio of ALR over CHCHD4 appear to correlate only weakly with the redox state, and although ALR is present in superstoichiometric amounts, it does not lead to fully oxidized CHCHD4.

Indexed as

AnimalsDisulfidesMiceMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOrgan SpecificityOxidation-ReductionOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProtein TransportChchd4 protein, mouseDisulfidesGFER protein, mouseMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsCHCHD4/ALR/disulfide/redox/mitochondria

Identifiers

PMID29704824
PMCPMC6007816
OpenAlexW2791283531

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.