ArticleEukaryotic cell2013
Atypical mitogen-activated protein kinase phosphatase implicated in regulating transition from pre-S-Phase asexual intraerythrocytic development of Plasmodium falciparum.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- A PPP-type pseudophosphatase is required for the maintenance of basal complex integrity in Plasmodium falciparum.Nature communications · 2023Article
- Deciphering the Role of Protein Phosphatases in Apicomplexa: The Future of Innovative Therapeutics?Microorganisms · 2022Review
- AttenuatedFrontiers in immunology · 2020Article
- Uncovering the essential genes of the human malaria parasiteScience (New York, N.Y.) · 2018Article
- Article
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
- In silico characterization of an atypical MAPK phosphatase of Plasmodium falciparum as a suitable target for drug discovery.Chemical biology & drug design · 2014Article
- Phenotypic Screens Identify Parasite Genetic Factors Associated with Malarial Fever Response inmSphereArticle
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Intraerythrocytic development of the human malaria parasite Plasmodium falciparum appears as a continuous flow through growth and proliferation. To develop a greater understanding of the critical regulatory events, we utilized piggyBac insertional mutagenesis to randomly disrupt genes. Screening a collection of piggyBac mutants for slow growth, we isolated the attenuated parasite C9, which carried a single insertion disrupting the open reading frame (ORF) of PF3D7_1305500. This gene encodes a protein structurally similar to a mitogen-activated protein kinase (MAPK) phosphatase, except for two notable characteristics that alter the signature motif of the dual-specificity phosphatase domain, suggesting that it may be a low-activity phosphatase or pseudophosphatase. C9 parasites demonstrated a significantly lower growth rate with delayed entry into the S/M phase of the cell cycle, which follows the stage of maximum PF3D7_1305500 expression in intact parasites. Genetic complementation with the full-length PF3D7_1305500 rescued the wild-type phenotype of C9, validating the importance of the putative protein phosphatase PF3D7_1305500 as a regulator of pre-S-phase cell cycle progression in P. falciparum.
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