ArticleMolecular and biochemical parasitology2017
NADH dehydrogenase of Trypanosoma brucei is important for efficient acetate production in bloodstream forms.
Article in Molecular and biochemical parasitology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Energy metabolism inmBio · 2025Review
- Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.Current protein & peptide science · 2025Review
- KREH2 helicase represses ND7 mRNA editing in procyclic-stage Trypanosoma brucei by opposite modulation of canonical and 'moonlighting' gRNA utilization creating a proposed mRNA structure.Nucleic acids research · 2024Article
- Trypanosome RNA helicase KREH2 differentially controls non-canonical editing and putative repressive structure via a novel proposed 'bifunctional' gRNA in mRNA A6.Nucleic acids research · 2023Article
- MICU1 and MICU2 potentiation of CaCell calcium · 2022Article
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- Divergent metabolism between Trypanosoma congolense and Trypanosoma brucei results in differential sensitivity to metabolic inhibition.PLoS pathogens · 2021Article
- Developmental regulation of edited CYb and COIII mitochondrial mRNAs is achieved by distinct mechanisms in Trypanosoma brucei.Nucleic acids research · 2020Article
- Mitochondrial DNA is critical for longevity and metabolism of transmission stage Trypanosoma brucei.PLoS pathogens · 2018Article
- A paradigm shift: The mitoproteomes of procyclic and bloodstream Trypanosoma brucei are comparably complex.PLoS pathogens · 2017Review
- Stunning Intricacies of RNA Editing Complexes RECC, RESC, and REH2C: Functional Organization, Developmental Regulation, and Evolutionary History in Kinetoplastid Protists.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
8 authors at 6 institutions in 3 countries.
Funding
Abstract
In the slender bloodstream form, Trypanosoma brucei mitochondria are repressed for many functions. Multiple components of mitochondrial complex I, NADH:ubiquinone oxidoreductase, are expressed in this stage, but electron transfer through complex I is not essential. Here we investigate the role of the parasite's second NADH:ubiquinone oxidoreductase, NDH2, which is composed of a single subunit that also localizes to the mitochondrion. While inducible knockdown of NDH2 had a modest growth effect in bloodstream forms, NDH2 null mutants, as well as inducible knockdowns in a complex I deficient background, showed a greater reduction in growth. Altering the NAD
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