Evidence map›Paper›PMID 28060946›Full record

ArticlePloS one2017

High Osmolarity Environments Activate the Mitochondrial Alternative Oxidase in Debaryomyces Hansenii.

Wilson Garcia-Neto, Alfredo Cabrera-Orefice, Salvador Uribe-Carvajal, Alicia J Kowaltowski, Luis Alberto Luévano-Martínez

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  4. Complex II ambiguities-FADHThe Journal of biological chemistry · 2024
    Review
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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

5 authors at 2 institutions in 2 countries.

Wilson Garcia-NetoDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.
Alfredo Cabrera-OreficeDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México, México.
Salvador Uribe-CarvajalDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México, México.
Alicia J KowaltowskiDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.
Luis Alberto Luévano-MartínezDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.
Universidade de São Paulo · BRUniversidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oleaginous yeast Debaryomyces hansenii is a good model to understand molecular mechanisms involved in halotolerance because of its impressive ability to survive under a wide range of salt concentrations. Several cellular adaptations are implicated in this response, including the presence of a cyanide-insensitive ubiquinol oxidase (Aox). This protein, which is present in several taxonomical orders, has been related to different stress responses. However, little is known about its role in mitochondria during transitions from low to high saline environments. In this report, we analyze the effects of Aox in shifts from low to high salt concentrations in the culture media. At early stages of a salt insult, we observed that this protein prevents the overflow of electrons on the mitochondrial respiratory chain, thus, decreasing the production of reactive oxygen species. Interestingly, in the presence of high osmolite concentrations, Aox activity is able to sustain a stable membrane potential when coupled to complex I, despite a compromised cytochrome pathway. Taken together, our results suggest that under high osmolarity conditions Aox plays a critical role regulating mitochondrial physiology.

Indexed as

Mitochondrial ProteinsOsmolar ConcentrationOxidoreductasesPlant ProteinsAlternative OxidaseAscomycotaCell RespirationCell SurvivalElectron TransportElectron Transport Chain Complex ProteinsMembrane Potential, MitochondrialMitochondriaOxidation-ReductionStress, PhysiologicalAlternative OxidaseElectron Transport Chain Complex ProteinsMitochondrial ProteinsOxidoreductasesPlant Proteins

Identifiers

PMID28060946
PMCPMC5218487
OpenAlexW2570386267

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.