Evidence map›Paper›PMID 26221731›Full record

ArticlePloS one2015

A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity.

Janet H C Yeo, Jarrod P J Skinner, Matthew J Bird, Luke E Formosa, Jian-Guo Zhang, Ruth M Kluck, Gabrielle T Belz, Mark M W Chong

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.3field-weighted citation impact, top 39% 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, 17 citations in OpenAlex.

  1. Article
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  11. Mitochondrial HSP90 Accumulation Promotes Vascular Remodeling in Pulmonary Arterial Hypertension.American journal of respiratory and critical care medicine · 2018
    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 1 country.

Janet H C YeoWalter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC, Australia; St. Vincent's Institute of Medical Research, Fitzroy, VIC, Australia.
Jarrod P J SkinnerSt. Vincent's Institute of Medical Research, Fitzroy, VIC, Australia.
Matthew J BirdMurdoch Childrens Research Institute, Parkville, VIC, Australia; Department of Paediatrics, University of Melbourne, Parkville VIC, Australia.
Luke E FormosaDepartment of Biochemistry, La Trobe University, Bundoora, VIC, Australia.
Jian-Guo ZhangWalter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC, Australia.
Ruth M KluckWalter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC, Australia.
Gabrielle T BelzWalter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC, Australia.
Mark M W ChongSt. Vincent's Institute of Medical Research, Fitzroy, VIC, Australia; Department of Medicine (St Vincent's), University of Melbourne, Parkville VIC, Australia.
St Vincents Institute of Medical Research · AUWalter and Eliza Hall Institute of Medical Research · AULa Trobe University · AUUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We identified Mrpl44 in a search for mammalian proteins that contain RNase III domains. This protein was previously found in association with the mitochondrial ribosome of bovine liver extracts. However, the precise Mrpl44 localization had been unclear. Here, we show by immunofluorescence microscopy and subcellular fractionation that Mrpl44 is localized to the matrix of the mitochondria. We found that it can form multimers, and confirm that it is part of the large subunit of the mitochondrial ribosome. By manipulating its expression, we show that Mrpl44 may be important for regulating the expression of mtDNA-encoded genes. This was at the level of RNA expression and protein translation. This ultimately impacted ATP synthesis capability and respiratory capacity of cells. These findings indicate that Mrpl44 plays an important role in the regulation of the mitochondrial OXPHOS capacity.

Indexed as

Adenosine TriphosphateAnimalsCattleCell LineDNA, MitochondrialGene Expression RegulationGene Knockdown TechniquesHEK293 CellsHumansMiceMitochondria, LiverMitochondrial ProteinsMitochondrial RibosomesNIH 3T3 CellsOxidative PhosphorylationOxygen ConsumptionAdenosine TriphosphateDNA, MitochondrialMitochondrial ProteinsRibonuclease IIIRibosomal Proteins

Identifiers

PMID26221731
PMCPMC4519308
OpenAlexW945440826

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.