ReviewOpen biology2020
Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.
Review in Open biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 67 citations in OpenAlex.
- Motif-guided trafficking of leishmanial PAS domain-containing phosphoglycerate kinase into glycosomes and lysosomes.FEBS letters · 2026Article
- Lack of evidence for the presence of plastids in the evolutionary history of kinetoplastid protists.Folia parasitologica · 2026Article
- PINK1‑mediated mitophagy enhances breast cancer proliferation through metabolic reprogramming.Oncology reports · 2026Article
- An Effective YOLOv11 Grain Detection Model Trained on Intact Barley Spikes Reveals a QTL Containing a Pivotal Regulator of Lateral Spikelet Formation.Plants (Basel, Switzerland) · 2026Article
- Protium heptaphyllum, a tree native to the Atlantic Forest, is a potential source of compounds against important cocoa phytopathogen.Scientific reports · 2026Article
- Characterization of GH18 chitinase in Leishmania braziliensis: expression, structural insights, and implications for vaccine and therapeutic development.Biological research · 2026Article
- Molecular characterization and functional effect on canie peripheral blood mononuclear cells of phosphoglycerate kinase from Echinococcus granulosus.Parasitology research · 2026Article
- The related EIF4G3 and EIF4G4 initiation factors from Leishmania: dissimilar modes of action during translation revealed by a comparative proteomic approach.Parasites & vectors · 2026Article
- Integrative Structural Characterization ofACS omega · 2026Article
- A novel transdermal curcumin gel shows potential in improving cardiac bioenergetic functions in Berkeley sickle cell mice.Blood vessels, thrombosis & hemostasis · 2026Article
- Chemoproteomics-based profiling elucidates the antimalarial effects of amodiaquine through disruption of glycolysis process in Plasmodium falciparum.Cell communication and signaling : CCS · 2026Article
- Validation of reference genes for RT-qPCR relative expression analysis during cyst-to-early adult development of Taenia solium.PLoS neglected tropical diseases · 2026Article
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- Role of Glycolysis and Nitric Oxide Pathway Crosstalk in Macrophages in Atherosclerosis.Current medicinal chemistry · 2026Review
- Transcriptional analysis of genes associated with glycolysis in Streptomyces coelicolor M145.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Dysregulated Expression of Canonical and Non-Canonical Glycolytic Enzyme Isoforms in Peripheral Blood from Subjects with Alcohol Use Disorder and from Individuals with Acute Alcohol Consumption.Antioxidants (Basel, Switzerland) · 2025Article
- Genome Sequences of the First Phages InfectingMicroorganisms · 2025Article
- Analysis of stress response in multiple bacterial pathogens using a network biology approach.Scientific reports · 2025Article
- Dimeric assembly of FScience advances · 2025Article
- Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoglycerate kinase (PGK) is a glycolytic enzyme that is well conserved among the three domains of life. PGK is usually a monomeric enzyme of about 45 kDa that catalyses one of the two ATP-producing reactions in the glycolytic pathway, through the conversion of 1,3-bisphosphoglycerate (1,3BPGA) to 3-phosphoglycerate (3PGA). It also participates in gluconeogenesis, catalysing the opposite reaction to produce 1,3BPGA and ADP. Like most other glycolytic enzymes, PGK has also been catalogued as a moonlighting protein, due to its involvement in different functions not associated with energy metabolism, which include pathogenesis, interaction with nucleic acids, tumorigenesis progression, cell death and viral replication. In this review, we have highlighted the overall aspects of this enzyme, such as its structure, reaction kinetics, activity regulation and possible moonlighting functions in different protistan organisms, especially both free-living and parasitic Kinetoplastea. Our analysis of the genomes of different kinetoplastids revealed the presence of open-reading frames (ORFs) for multiple PGK isoforms in several species. Some of these ORFs code for unusually large PGKs. The products appear to contain additional structural domains fused to the PGK domain. A striking aspect is that some of these PGK isoforms are predicted to be catalytically inactive enzymes or 'dead' enzymes. The roles of PGKs in kinetoplastid parasites are analysed, and the apparent significance of the PGK gene duplication that gave rise to the different isoforms and their expression in
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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 Socratic graph.