ReviewMicrobiology and molecular biology reviews : MMBR2008
Possible effects of microbial ecto-nucleoside triphosphate diphosphohydrolases on host-pathogen interactions.
Review in Microbiology and molecular biology reviews : MMBR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
40 citing papers in PubMed, 87 citations in OpenAlex.
- Comparison of Aroma and Taste Profiles of Pixian Douban Fermented with Traditional Open Process or Industrial Closed Process.Foods (Basel, Switzerland) · 2026Article
- Synthesis of new non-natural L-glycosidic flavonoid derivatives and their evaluation as inhibitors of Trypanosoma cruzi ecto-nucleoside triphosphate diphosphohydrolase 1 (TcNTPDase1).Purinergic signalling · 2024Article
- Overexpression ofInternational journal of molecular sciences · 2022Article
- Enzyme histochemistry: a useful tool for examining the spatial distribution of brain ectonucleotidases in (patho)physiological conditions.Histology and histopathology · 2022Review
- Mining the Proteome ofAnimals : an open access journal from MDPI · 2022Review
- The Ecto-5'nucleotidase/CD73 MediatesBioMed research international · 2022Article
- E-NTPDases: Possible Roles on Host-Parasite Interactions and Therapeutic Opportunities.Frontiers in cellular and infection microbiology · 2021Review
- Trichomonas vaginalis NTPDase inhibited by lycorine modulates the parasite-neutrophil interaction.Parasitology research · 2020Article
- Knocking Down TcNTPDase-1 Gene ReducesFrontiers in microbiology · 2020Article
- Koala and Wombat Gammaherpesviruses Encode the First Known Viral NTPDase Homologs and Are Phylogenetically Divergent from All Known Gammaherpesviruses.Journal of virology · 2019Article
- Review
- Purinergic Antagonist Suramin Aggravates Myocarditis and Increases Mortality by Enhancing Parasitism, Inflammation, and Reactive Tissue Damage inOxidative medicine and cellular longevity · 2018Article
- Plasmodium falciparum GFP-E-NTPDase expression at the intraerythrocytic stages and its inhibition blocks the development of the human malaria parasite.Purinergic signalling · 2017Article
- Purinergic signaling during intestinal inflammation.Journal of molecular medicine (Berlin, Germany) · 2017Review
- Apyrase inhibitors enhance the ability of diverse fungicides to inhibit the growth of different plant-pathogenic fungi.Molecular plant pathology · 2017Article
- Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.Protein science : a publication of the Protein Society · 2017Article
- Infection of Human Macrophages byFrontiers in immunology · 2017Article
- Trichomoniasis immunity and the involvement of the purinergic signaling.Biomedical journal · 2016Review
- Regulation of the T Cell Response by CD39.Trends in immunology · 2016Review
- Immobilization of NTPDase-1 fromJournal of analytical methods in chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
In humans, purinergic signaling plays an important role in the modulation of immune responses through specific receptors that recognize nucleoside tri- and diphosphates as signaling molecules. Ecto-nucleoside triphosphate diphosphohydrolases (ecto-NTPDases) have important roles in the regulation of purinergic signaling by controlling levels of extracellular nucleotides. This process is key to pathophysiological protective responses such as hemostasis and inflammation. Ecto-NTPDases are found in all higher eukaryotes, and recently it has become apparent that a number of important parasitic pathogens of humans express surface-located NTPDases that have been linked to virulence. For those parasites that are purine auxotrophs, these enzymes may play an important role in purine scavenging, although they may also influence the host response to infection. Although ecto-NTPDases are rare in bacteria, expression of a secreted NTPDase in Legionella pneumophila was recently described. This ecto-enzyme enhances intracellular growth of the bacterium and potentially affects virulence. This discovery represents an important advance in the understanding of the contribution of other microbial NTPDases to host-pathogen interactions. Here we review other progress made to date in the characterization of ecto-NTPDases from microbial pathogens, how they differ from mammalian enzymes, and their association with organism viability and virulence. In addition, we postulate how ecto-NTPDases may contribute to the host-pathogen interaction by reviewing the effect of selected microbial pathogens on purinergic signaling. Finally, we raise the possibility of targeting ecto-NTPDases in the development of novel anti-infective agents based on potential structural and clear enzymatic differences from the mammalian ecto-NTPDases.
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.