ReviewTrends in parasitology2005
A glycine-cleavage complex as part of the folate one-carbon metabolism of Plasmodium falciparum.
Review in Trends in parasitology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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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.
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Who cites it
18 citing papers in PubMed, 43 citations in OpenAlex.
- The mitochondrion ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Roles of Mitochondrial Folate Metabolism in Supporting Mitochondrial DNA Synthesis, Oxidative Phosphorylation, and Cellular Function.Current developments in nutrition · 2020Article
- Article
- Article
- The Uptake and Metabolism of Amino Acids, and Their Unique Role in the Biology of Pathogenic Trypanosomatids.Pathogens (Basel, Switzerland) · 2018Review
- A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species.Molecular microbiology · 2017Article
- Novel Plasmodium falciparum metabolic network reconstruction identifies shifts associated with clinical antimalarial resistance.BMC genomics · 2017Article
- Redox-dependent lipoylation of mitochondrial proteins in Plasmodium falciparum.Molecular microbiology · 2014Article
- Vitamin B6-dependent enzymes in the human malaria parasite Plasmodium falciparum: a druggable target?BioMed research international · 2014Review
- Plasmodium serine hydroxymethyltransferase: indispensability and display of distinct localization.Malaria journal · 2012Article
- Lipoic acid metabolism of Plasmodium--a suitable drug target.Current pharmaceutical design · 2012Review
- Dynamic subcellular localization of isoforms of the folate pathway enzyme serine hydroxymethyltransferase (SHMT) through the erythrocytic cycle of Plasmodium falciparum.Malaria journal · 2010Article
- Validation of a modified method for Bxb1 mycobacteriophage integrase-mediated recombination in Plasmodium falciparum by localization of the H-protein of the glycine cleavage complex to the mitochondrion.Molecular and biochemical parasitology · 2010Article
- Lipoic acid metabolism in microbial pathogens.Microbiology and molecular biology reviews : MMBR · 2010Review
- Catalytic and ligand-binding characteristics of Plasmodium falciparum serine hydroxymethyltransferase.Molecular and biochemical parasitology · 2009Article
- Targeting purine and pyrimidine metabolism in human apicomplexan parasites.Current drug targets · 2007Review
- Proteins of the glycine decarboxylase complex in the hydrogenosome of Trichomonas vaginalis.Eukaryotic cell · 2006Article
- Apicoplast fatty acid synthesis is essential for organelle biogenesis and parasite survival in Toxoplasma gondii.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The glycine-cleavage complex (GCV) and serine hydroxymethyltransferase represent the two systems of one-carbon transfer that are employed in the biosynthesis of active folate cofactors in eukaryotes. Although the understanding of this area of metabolism in Plasmodium falciparum is still at an early stage, we discuss evidence that genes and transcription products of the GCV are present and expressed in this parasite. The potential role of the GCV and its relevance to the life cycle and pathogenesis of the malaria erythrocytic stages are also considered. According to its expression profile, the GCV seems to be particularly active in gametocytes. The GCV enzyme dihydrolipoamide dehydrogenase has two isoforms encoded by two different genes. It has been demonstrated recently that both genes are functional, with one of them identified as being part of a pyruvate dehydrogenase complex that is present exclusively in the apicoplast of Plasmodium species. The other isoform probably forms part of the Plasmodium GCV. The GCV is the first enzyme complex involved in folate metabolism in this parasite that can be assumed, with a good degree of certainty, to be located in the mitochondria.
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What OpenQuestion holds
Registered trials
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.