ArticleMolecular and biochemical parasitology2007
Kinetoplastid PPEF phosphatases: dual acylated proteins expressed in the endomembrane system of Leishmania.
Article in Molecular and biochemical parasitology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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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Who cites it
36 citing papers in PubMed, 56 citations in OpenAlex.
- C. elegans PPEF-type phosphatase (Retinal degeneration C ortholog) functions in diverse classes of cilia to regulate nematode behaviors.Scientific reports · 2024Article
- Tackling Sleeping Sickness: Current and Promising Therapeutics and Treatment Strategies.International journal of molecular sciences · 2023Review
- Global distribution of treatment resistance gene markers for leishmaniasis.Journal of clinical laboratory analysis · 2022Review
- Parasite protein phosphatases: biological function, virulence, and host immune evasion.Parasitology research · 2021Review
- Involvement ofFrontiers in cellular and infection microbiology · 2021Review
- Novel Thienopyrimidine Inhibitors ofJournal of medicinal chemistry · 2020Article
- Small Myristoylated Protein-3, Identified as a Potential Virulence Factor in Leishmania amazonensis, Proves to be a Protective Antigen against Visceral Leishmaniasis.International journal of molecular sciences · 2018Article
- Dynamic protein S-palmitoylation mediates parasite life cycle progression and diverse mechanisms of virulence.Critical reviews in biochemistry and molecular biology · 2017Review
- Function of Macrophage and Parasite Phosphatases in Leishmaniasis.Frontiers in immunology · 2017Review
- KHARON Is an Essential Cytoskeletal Protein Involved in the Trafficking of Flagellar Membrane Proteins and Cell Division in African Trypanosomes.The Journal of biological chemistry · 2016Article
- The N-myristoylome of Trypanosoma cruzi.Scientific reports · 2016Article
- Global Profiling and Inhibition of Protein Lipidation in Vector and Host Stages of the Sleeping Sickness ParasiteACS infectious diseases · 2016Article
- Cos-Seq for high-throughput identification of drug target and resistance mechanisms in the protozoan parasite Leishmania.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Validation of N-myristoyltransferase as Potential Chemotherapeutic Target in Mammal-Dwelling Stages of Trypanosoma cruzi.PLoS neglected tropical diseases · 2016Article
- Flagellar membrane proteins in kinetoplastid parasites.IUBMB life · 2015Review
- Ca2+ Regulation of Trypanosoma brucei Phosphoinositide Phospholipase C.Eukaryotic cell · 2015Article
- Global analysis of protein N-myristoylation and exploration of N-myristoyltransferase as a drug target in the neglected human pathogen Leishmania donovani.Chemistry & biology · 2015Article
- A target repurposing approach identifies N-myristoyltransferase as a new candidate drug target in filarial nematodes.PLoS neglected tropical diseases · 2014Article
- Acylation in trypanosomatids: an essential process and potential drug target.Trends in parasitology · 2014Review
- Biochemical and genetic characterization of Trypanosoma cruzi N-myristoyltransferase.The Biochemical journal · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Bioinformatic analyses have been used to identify potential downstream targets of the essential enzyme N-myristoyl transferase in the TriTryp species, Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. These database searches predict approximately 60 putative N-myristoylated proteins with high confidence, including both previously characterised and novel molecules. One of the latter is an N-myristoylated protein phosphatase which has high sequence similarity to the Protein Phosphatase with EF-Hand (PPEF) proteins identified in sensory cells of higher eukaryotes. In L. major and T. brucei, the PPEF-like phosphatases are encoded by single-copy genes and are constitutively expressed in all parasite life cycle stages. The N-terminus of LmPPEF is a substrate for N-myristoyl transferase and is also palmitoylated in vivo. The wild type protein has been localised to the endocytic system by immunofluorescence. The catalytic and fused C-terminal domains of the kinetoplastid and other eukaryotic PPEFs share high sequence similarity, but unlike their higher eukaryotic relatives, the C-terminal parasite EF-hand domains are degenerate and do not bind calcium.
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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.