ReviewFrontiers in pharmacology2014
Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy.
Review in Frontiers in pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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.
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
15 citing papers in PubMed, 34 citations in OpenAlex.
- Anandamide Targets Membrane Integrity in Non-Journal of fungi (Basel, Switzerland) · 2026Article
- The V-ATPase VJournal of oral microbiology · 2026Article
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Article
- Carvacrol-Induced Vacuole Dysfunction and Morphological Consequences inMicroorganisms · 2023Article
- The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020Review
- Vacuolar proton-translocating ATPase is required for antifungal resistance and virulence of Candida glabrata.PloS one · 2019Article
- Atovaquone Impairs Growth of Aspergillus and Fusarium Keratitis Isolates by Modulating Mitochondrial Function and Zinc Homeostasis.Investigative ophthalmology & visual science · 2018Article
- FcRav2, a gene with a ROGDI domain involved in Fusarium head blight and crown rot on durum wheat caused by Fusarium culmorum.Molecular plant pathology · 2018Article
- Rotation Mechanism of Molecular Motor VBiophysical journal · 2017Article
- Proton Transport and pH Control in Fungi.Advances in experimental medicine and biology · 2016Review
- Identification of Additional Anti-Persister Activity against Borrelia burgdorferi from an FDA Drug Library.Antibiotics (Basel, Switzerland) · 2015Article
- The contribution of Candida albicans vacuolar ATPase subunit V₁B, encoded by VMA2, to stress response, autophagy, and virulence is independent of environmental pH.Eukaryotic cell · 2014Article
- Saccharomyces cerevisiae vacuolar H+-ATPase regulation by disassembly and reassembly: one structure and multiple signals.Eukaryotic cell · 2014Review
- Attenuation of Candida albicans virulence with focus on disruption of its vacuole functions.Journal of oral microbiology · 2014Review
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 1 country.
Funding
Abstract
Vacuolar proton-translocating ATPase (V-ATPase) is a membrane-bound, multi-subunit enzyme that uses the energy of ATP hydrolysis to pump protons across membranes. V-ATPase activity is critical for pH homeostasis and organelle acidification as well as for generation of the membrane potential that drives secondary transporters and cellular metabolism. V-ATPase is highly conserved across species and is best characterized in the model fungus Saccharomyces cerevisiae. However, recent studies in mammals have identified significant alterations from fungi, particularly in the isoform composition of the 14 subunits and in the regulation of complex disassembly. These differences could be exploited for selectivity between fungi and humans and highlight the potential for V-ATPase as an anti-fungal drug target. Candida albicans is a major human fungal pathogen and causes fatality in 35% of systemic infections, even with anti-fungal treatment. The pathogenicity of C. albicans correlates with environmental, vacuolar, and cytoplasmic pH regulation, and V-ATPase appears to play a fundamental role in each of these processes. Genetic loss of V-ATPase in pathogenic fungi leads to defective virulence, and a comprehensive picture of the mechanisms involved is emerging. Recent studies have explored the practical utility of V-ATPase as an anti-fungal drug target in C. albicans, including pharmacological inhibition, azole therapy, and targeting of downstream pathways. This overview will discuss these studies as well as hypothetical ways to target V-ATPase and novel high-throughput methods for use in future drug discovery screens.
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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.