ArticleNature communications2015
Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
Who cites it
110 citing papers in PubMed, 1 synthesis or guideline pooled it, 191 citations in OpenAlex.
- Phosphorylation in theJournal of proteome research · 2024Pooled it
- Origins and Molecular Features of a Chimeric Type-P4A ATPase-Guanylate Cyclase from Stramenopiles and Alveolates.International journal of molecular sciences · 2026Article
- Cross-species therapeutics in Plasmodium and Babesia: erythrocyte invasion and conserved drug targets.Tropical animal health and production · 2026Review
- An orally available PfPKG inhibitor blocks Plasmodium's infection of the liver.PLoS pathogens · 2026Article
- A role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5.Nature communications · 2026Article
- Phosphorylation shapes antigen presentation and immune recognition: mechanistic insights and translational perspectives.Frontiers in immunology · 2026Review
- Physiology of invasiveFrontiers in cellular and infection microbiology · 2026Review
- Key Regulators of Parasite Biology Viewed Through a Post-Translational Modification Repertoire.Proteomics · 2025Review
- Emerging Molecular Mechanisms in Malaria Pathogenesis and Novel Therapeutic Approaches: A Focus onBiomolecules · 2025Review
- Covalent inhibition ofiScience · 2025Article
- Unveiling the impact of cGMP-dependent protein kinase of Neospora caninum on calcium fluxes and egress functions through quantitative phosphoproteome analysis.Communications biology · 2025Article
- Phospho-relay feedback loops control egress vs. intracellular development in Toxoplasma gondii.Cell reports · 2025Article
- Proteomic approaches for protein kinase substrate identification in Apicomplexa.Molecular and biochemical parasitology · 2024Review
- SPARK regulates AGC kinases central to theeLife · 2024Article
- Activation loop phosphorylation and cGMP saturation of PKG regulate egress of malaria parasites.PLoS pathogens · 2024Article
- SPARK regulates AGC kinases central to thebioRxiv : the preprint server for biology · 2024Article
- Review
- Glycosylation in malaria parasites: what do we know?Trends in parasitology · 2024Review
- Protein Lactylation and Metabolic Regulation of the Zoonotic Parasite Toxoplasma gondii.Genomics, proteomics & bioinformatics · 2023Article
- Analysis of CDPK1 targets identifies a trafficking adaptor complex that regulates microneme exocytosis ineLife · 2023Article
50 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
17 authors at 5 institutions in 4 countries.
Funding
Abstract
Our understanding of the key phosphorylation-dependent signalling pathways in the human malaria parasite, Plasmodium falciparum, remains rudimentary. Here we address this issue for the essential cGMP-dependent protein kinase, PfPKG. By employing chemical and genetic tools in combination with quantitative global phosphoproteomics, we identify the phosphorylation sites on 69 proteins that are direct or indirect cellular targets for PfPKG. These PfPKG targets include proteins involved in cell signalling, proteolysis, gene regulation, protein export and ion and protein transport, indicating that cGMP/PfPKG acts as a signalling hub that plays a central role in a number of core parasite processes. We also show that PfPKG activity is required for parasite invasion. This correlates with the finding that the calcium-dependent protein kinase, PfCDPK1, is phosphorylated by PfPKG, as are components of the actomyosin complex, providing mechanistic insight into the essential role of PfPKG in parasite egress and invasion.
Indexed as
Identifiers
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.