Evidence map›Paper›PMID 33551002›Full record

ReviewParasitology2021

Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase.

Ondřej Gahura, Carolina Hierro-Yap, Alena Zíková

Abstract readReview
In one paragraph

Review in Parasitology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
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  5. 3-Bromopyruvate Impairs Mitochondrial Function inPathogens (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Iron Uptake ControlsAntioxidants (Basel, Switzerland) · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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

3 authors.

Ondřej GahuraBiology Centre, Czech Academy of Sciences, Branišovská 31, České Budějovice, 37005, Czech Republic.ORCID 0000-0002-2925-4763
Carolina Hierro-YapBiology Centre, Czech Academy of Sciences, Branišovská 31, České Budějovice, 37005, Czech Republic.
Alena ZíkováBiology Centre, Czech Academy of Sciences, Branišovská 31, České Budějovice, 37005, Czech Republic.ORCID 0000-0002-8686-0225

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial F-type adenosine triphosphate (ATP) synthases are commonly introduced as highly conserved membrane-embedded rotary machines generating the majority of cellular ATP. This simplified view neglects recently revealed striking compositional diversity of the enzyme and the fact that in specific life stages of some parasites, the physiological role of the enzyme is to maintain the mitochondrial membrane potential at the expense of ATP rather than to produce ATP. In addition, mitochondrial ATP synthases contribute indirectly to the organelle's other functions because they belong to major determinants of submitochondrial morphology. Here, we review current knowledge about the trypanosomal ATP synthase composition and architecture in the context of recent advances in the structural characterization of counterpart enzymes from several eukaryotic supergroups. We also discuss the physiological function of mitochondrial ATP synthases in three trypanosomatid parasites, Trypanosoma cruzi, Trypanosoma brucei and Leishmania, with a focus on their disease-causing life cycle stages. We highlight the reversed proton-pumping role of the ATP synthase in the T. brucei bloodstream form, the enzyme's potential link to the regulation of parasite's glycolysis and its role in generating mitochondrial membrane potential in the absence of mitochondrial DNA.

Indexed as

Genetic EngineeringLeishmaniaMembrane Potential, MitochondrialMitochondrial Proton-Translocating ATPasesProtozoan ProteinsTrypanosoma brucei bruceiTrypanosoma cruziMitochondrial Proton-Translocating ATPasesProtozoan ProteinsATP synthasecryo-EMmitochondriamitochondrial membrane potentialoxidative phosphorylation

Identifiers

PMID33551002
PMCPMC8311965

What OpenQuestion holds

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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.