Evidence map›Paper›PMID 29413965›Full record

ArticleRedox biology2018

A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.

Samantha Ebersoll, Blessing Musunda, Torsten Schmenger, Natalie Dirdjaja, Mariana Bonilla, Bruno Manta, Kathrin Ulrich, Marcelo A Comini, R Luise Krauth-Siegel

Open access · goldAbstract read
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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.0field-weighted citation impact, top 9% 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, 22 citations in OpenAlex.

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  4. Identification and Function of Apicoplast Glutaredoxins inInternational journal of molecular sciences · 2021
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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

9 authors at 2 institutions in 2 countries.

Samantha EbersollBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Blessing MusundaBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Torsten SchmengerBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Natalie DirdjajaBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Mariana BonillaGroup Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.
Bruno MantaGroup Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.
Kathrin UlrichBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Marcelo A CominiGroup Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.
R Luise Krauth-SiegelBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. Electronic address: luise.krauth-siegel@bzh.uni-heidelberg.de.
Heidelberg University · DEInstitut Pasteur de Montevideo · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trypanosoma brucei glutaredoxin 2 (Grx2) is a dithiol glutaredoxin that is specifically located in the mitochondrial intermembrane space. Bloodstream form parasites lacking Grx2 or both, Grx2 and the cytosolic Grx1, are viable in vitro and infectious to mice suggesting that neither oxidoreductase is needed for survival or infectivity to mammals. A 37 °C to 39 °C shift changes the cellular redox milieu of bloodstream cells to more oxidizing conditions and induces a significantly stronger growth arrest in wildtype parasites compared to the mutant cells. Grx2-deficient cells ectopically expressing the wildtype form of Grx2 with its C31QFC34 active site, but not the C34S mutant, regain the sensitivity of the parental strain, indicating that the physiological role of Grx2 requires both active site cysteines. In the procyclic insect stage of the parasite, Grx2 is essential. Both alleles can be replaced if procyclic cells ectopically express authentic or C34S, but not C31S/C34S Grx2, pointing to a redox role that relies on a monothiol mechanism. RNA-interference against Grx2 causes a virtually irreversible proliferation defect. The cells adopt an elongated morphology but do not show any significant alteration in the cell cycle. The growth retardation is attenuated by high glucose concentrations. Under these conditions, procyclic cells obtain ATP by substrate level phosphorylation suggesting that Grx2 might regulate a respiratory chain component.

Indexed as

Adaptation, PhysiologicalAdenosine TriphosphateAllelesAnimalsCatalytic DomainCell ProliferationCytosolGlutaredoxinsHot TemperatureHumansMiceMitochondriaMitochondrial MembranesMutationOxidation-ReductionTrypanosoma brucei bruceiAdenosine TriphosphateGlutaredoxinsGlutaredoxinMitochondrionTrypanosoma bruceiTrypanothioneTryparedoxin

Identifiers

PMID29413965
PMCPMC5975080
OpenAlexW2791972889

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.