ArticlePloS one2013
Analysis of the Protein phosphotome of Entamoeba histolytica reveals an intricate phosphorylation network.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 11 citations in OpenAlex.
- Theoretical Study of Sphingomyelinases fromPathogens (Basel, Switzerland) · 2025Article
- Article
- Structure-Function Relationship Study of a Secretory Amoebic Phosphatase: A Computational-Experimental Approach.International journal of molecular sciences · 2021Article
- Protein Phosphatase PP2C Identification inBioMed research international · 2021Article
- Article
- Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB.PloS one · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Phosphorylation is the most common mechanism for the propagation of intracellular signals. Protein phosphatases and protein kinases play a dynamic antagonistic role in protein phosphorylation. Protein phosphatases make up a significant fraction of eukaryotic proteome. In this article, we report the identification and analysis of protein phosphatases in the intracellular parasite Entamoeba histolytica. Based on an in silico analysis, we classified 250 non-redundant protein phosphatases in E. histolytica. The phosphotome of E. histolytica is 3.1% of its proteome and 1.3 times of the human phosphotome. In this extensive study, we identified 42 new putative phosphatases (39 hypothetical proteins and 3 pseudophosphatases). The presence of pseudophosphatases may have an important role in virulence of E. histolytica. A comprehensive phosphotome analysis of E. histolytica shows spectacular low similarity to human phosphatases, making them potent candidates for drug target.
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