ArticlePurinergic signalling2011
The GDA1_CD39 superfamily: NTPDases with diverse functions.
Article in Purinergic signalling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 165 citations in OpenAlex.
- ENTPD3 as a novel regulator of endometrial receptivity: suppressing EMT via the ATP-P2Y2 axis in patients with recurrent implantation failure.Cellular & molecular biology letters · 2026Article
- Ecto-5'-nucleotidase/CD73 reduces COX-2 expression in activated macrophages.Scientific reports · 2026Article
- Levels of extracellular ATP in growth zones of Arabidopsis primary roots are changed by altered expression of apyrase enzymes.Plant signaling & behavior · 2025Article
- Chromatin-Associated Pea Apyrase psNTP9 Function as a DNA-Binding Regulatory Protein in Yeast and Arabidopsis.Plants (Basel, Switzerland) · 2025Article
- Structural Modeling of NTPDase-Substrate Complexes Preserving Catalytic Experimental Features.ACS omega · 2025Article
- Apyrase in horticultural crops: insights into growth, stress adaptation and quality regulation.Molecular horticulture · 2025Review
- Genome-Wide Analysis of Soybean Apyrase Gene Family and Functional Characterization of GmAPY1-4 Responses to Aluminum Stress.International journal of molecular sciences · 2025Article
- Evaluation of Synthetic Peptides fromACS infectious diseases · 2025Article
- Heterologous expression and biochemical characterization of the recombinant nucleoside triphosphate diphosphohydrolase 2 (LbNTPDase2) from Leishmania (Viannia) braziliensis.Purinergic signalling · 2024Article
- Article
- Genome-wide identification and analyses ofMolecular breeding : new strategies in plant improvement · 2024Article
- Growth regulation by apyrases: Insights from altering their expression level in different organisms.Plant physiology · 2024Review
- Growth-inhibiting effects of the unconventional plant APYRASE 7 of Arabidopsis thaliana influences the LRX/RALF/FER growth regulatory module.PLoS genetics · 2024Article
- Polarized distribution of extracellular nucleotides promotes gravity-directed polarization of development in spores ofFrontiers in plant science · 2023Article
- Article
- Delineating Purinergic Signaling inInternational journal of molecular sciences · 2022Review
- Enzyme histochemistry: a useful tool for examining the spatial distribution of brain ectonucleotidases in (patho)physiological conditions.Histology and histopathology · 2022Review
- Mechanosensitive Hydrolysis of ATP and ADP in Lamina Propria of the Murine Bladder by Membrane-Bound and Soluble Nucleotidases.Frontiers in physiology · 2022Article
- Extracellular ectonucleotidases are differentially regulated in murine tissues and human polymorphonuclear leukocytes during sepsis and inflammation.Purinergic signalling · 2021Article
- ENTPD5: identification of splicing variants and their impact on cancer survival.Purinergic signalling · 2021Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first comprehensive review of the ubiquitous "ecto-ATPases" by Plesner was published in 1995. A year later, a lymphoid cell activation antigen, CD39, that had been cloned previously, was shown to be an ecto-ATPase. A family of proteins, related to CD39 and a yeast GDPase, all containing the canonical apyrase conserved regions in their polypeptides, soon started to expand. They are now recognized as members of the GDA1_CD39 protein family. Because proteins in this family hydrolyze nucleoside triphosphates and diphosphates, a unifying nomenclature, nucleoside triphosphate diphopshohydrolases (NTPDases), was established in 2000. Membrane-bound NTPDases are either located on the cell surface or membranes of intracellular organelles. Soluble NTPDases exist in the cytosol and may be secreted. In the last 15 years, molecular cloning and functional expression have facilitated biochemical characterization of NTPDases of many organisms, culminating in the recent structural determination of the ecto-domain of a mammalian cell surface NTPDase and a bacterial NTPDase. The first goal of this review is to summarize the biochemical, mutagenesis, and structural studies of the NTPDases. Because of their ability in hydrolyzing extracellular nucleotides, the mammalian cell surface NTPDases (the ecto-NTPDases) which regulate purinergic signaling have received the most attention. Less appreciated are the functions of intracellular NTPDases and NTPDases of other organisms, e.g., bacteria, parasites, Drosophila, plants, etc. The second goal of this review is to summarize recent findings which demonstrate the involvement of the NTPDases in multiple and diverse physiological processes: pathogen-host interaction, plant growth, eukaryote cell protein and lipid glycosylation, eye development, and oncogenesis.
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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.