ArticleCell host & microbe2011
The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries.
Article in Cell host & microbe, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers, 1 of them a synthesis that pooled it.
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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
248 citing papers in PubMed, 1 synthesis or guideline pooled it, 415 citations in OpenAlex.
- Phosphorylation in theJournal of proteome research · 2024Pooled it
- Stage-specific proteomic and phosphoproteomic remodeling in Theileria annulata.Parasitology research · 2026Article
- A single valine to leucine switch disrupts Plasmodium falciparum AP2-G DNA binding and reveals GDV1's role in ap2-g activation.Nature communications · 2026Article
- Key Regulators of Parasite Biology Viewed Through a Post-Translational Modification Repertoire.Proteomics · 2025Review
- Article
- Ribosome-Associated Quality Control Mediated by Rqc2 Contributes to the Lytic Cycle and Stage Conversion ofMicroorganisms · 2025Article
- Emerging Molecular Mechanisms in Malaria Pathogenesis and Novel Therapeutic Approaches: A Focus onBiomolecules · 2025Review
- The fast-evolving FIKK kinase family of Plasmodium falciparum can be inhibited by a single compound.Nature microbiology · 2025Article
- Article
- Phospho-relay feedback loops control egress vs. intracellular development in Toxoplasma gondii.Cell reports · 2025Article
- The malaria parasite PP1 phosphatase controls the initiation of the egress pathway of asexual blood-stages by regulating the rounding-up of the vacuole.PLoS pathogens · 2025Article
- Article
- The essential kinase TgGSK regulates centrosome division and endodyogeny inbioRxiv : the preprint server for biology · 2024Article
- PP1 phosphatase controls both daughter cell formation and amylopectin levels in Toxoplasma gondii.PLoS biology · 2024Article
- BCC0 collaborates with IMC32 and IMC43 to form the Toxoplasma gondii essential daughter bud assembly complex.PLoS pathogens · 2024Article
- PfHDAC1 is an essential regulator ofmBio · 2024Article
- Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle.International journal of molecular sciences · 2024Review
- Activation loop phosphorylation and cGMP saturation of PKG regulate egress of malaria parasites.PLoS pathogens · 2024Article
- ToxoNet: A high confidence map of protein-protein interactions in Toxoplasma gondii.PLoS computational biology · 2024Article
- Toxoplasma protein export and effector function.Nature microbiology · 2024Review
188 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
4 authors at 1 institution in 1 country.
Funding
Abstract
Plasmodium falciparum and Toxoplasma gondii are obligate intracellular apicomplexan parasites that rapidly invade and extensively modify host cells. Protein phosphorylation is one mechanism by which these parasites can control such processes. Here we present a phosphoproteome analysis of peptides enriched from schizont stage P. falciparum and T. gondii tachyzoites that are either "intracellular" or purified away from host material. Using liquid chromatography-tandem mass spectrometry, we identified over 5,000 and 10,000 previously unknown phosphorylation sites in P. falciparum and T. gondii, respectively, revealing that protein phosphorylation is an extensively used regulation mechanism both within and beyond parasite boundaries. Unexpectedly, both parasites have phosphorylated tyrosines, and P. falciparum has unusual phosphorylation motifs that are apparently shaped by its A:T-rich genome. This data set provides important information on the role of phosphorylation in the host-pathogen interaction and clues to the evolutionary forces operating on protein phosphorylation motifs in both parasites.
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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.