Evidence map›Paper›PMID 25781180›Full record

ArticlePloS one2015

Detailed analysis of the human mitochondrial contact site complex indicate a hierarchy of subunits.

Christine Ott, Eva Dorsch, Martin Fraunholz, Sebastian Straub, Vera Kozjak-Pavlovic

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

75 citing papers in PubMed, 143 citations in OpenAlex.

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  10. Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025
    Review
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15 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

5 authors at 1 institution in 1 country.

Christine OttBiocenter, Chair of Microbiology, University of Würzburg, Am Hubland, Würzburg, Germany.
Eva DorschBiocenter, Chair of Microbiology, University of Würzburg, Am Hubland, Würzburg, Germany.
Martin FraunholzBiocenter, Chair of Microbiology, University of Würzburg, Am Hubland, Würzburg, Germany.
Sebastian StraubBiocenter, Chair of Microbiology, University of Würzburg, Am Hubland, Würzburg, Germany.
Vera Kozjak-PavlovicBiocenter, Chair of Microbiology, University of Würzburg, Am Hubland, Würzburg, Germany.
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial inner membrane folds into cristae, which significantly increase its surface and are important for mitochondrial function. The stability of cristae depends on the mitochondrial contact site (MICOS) complex. In human mitochondria, the inner membrane MICOS complex interacts with the outer membrane sorting and assembly machinery (SAM) complex, to form the mitochondrial intermembrane space bridging complex (MIB). We have created knockdown cell lines of most of the MICOS and MIB components and have used them to study the importance of the individual subunits for the cristae formation and complex stability. We show that the most important subunits of the MIB complex in human mitochondria are Mic60/Mitofilin, Mic19/CHCHD3 and an outer membrane component Sam50. We provide additional proof that ApoO indeed is a subunit of the MICOS and MIB complexes and propose the name Mic23 for this protein. According to our results, Mic25/CHCHD6, Mic27/ApoOL and Mic23/ApoO appear to be periphery subunits of the MICOS complex, because their depletion does not affect cristae morphology or stability of other components.

Indexed as

Protein MultimerizationApolipoproteinsHeLa CellsHumansMembrane ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProtein BindingProtein SubunitsApolipoproteinsAPOOL protein, humanAPOO protein, humanCHCHD3 protein, humanCHCHD6 protein, humanMembrane ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProtein SubunitsSAMM50 protein, human

Identifiers

PMID25781180
PMCPMC4363703
OpenAlexW2132909908

What OpenQuestion holds

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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.