ReviewThe Journal of membrane biology2016
The c-Ring of the F1FO-ATP Synthase: Facts and Perspectives.
Review in The Journal of membrane biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Mitochondrial permeability transition pore desensitization by a novel dispiranic derivative prevents cardiac reperfusion injury.Redox biology · 2026Article
- Calcium signaling in postsynaptic mitochondria: mechanisms, dynamics, and role in ATP production.Frontiers in molecular neuroscience · 2025Review
- Modeling control and transduction of electrochemical gradients in acid-stressed bacteria.iScience · 2023Article
- EngineeRING the gear of ATP synthase: a way to address complexity and flexibility of photosynthesis.Plant physiology · 2023Article
- 1,3,8-Triazaspiro[4.5]decane Derivatives Inhibit Permeability Transition Pores through a FInternational journal of molecular sciences · 2023Article
- Protein folding and unfolding: proline cis-trans isomerization at the c subunits of FProteins · 2022Article
- Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic bacteria and plant life.Extremophiles : life under extreme conditions · 2020Article
- Review
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- Direct assignment ofJournal of biomolecular NMR · 2018Article
- The Contribution of Different Components in QiShenYiQi Pills® to Its Potential to Modulate Energy Metabolism in Protection of Ischemic Myocardial Injury.Frontiers in physiology · 2018Article
- A Therapeutic Connection between Dietary Phytochemicals and ATP Synthase.Current medicinal chemistry · 2017Review
- Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 2017Article
- Cardioprotective Effect of Danshensu against Ischemic/Reperfusion Injury via c-Subunit of ATP Synthase Inhibition.Evidence-based complementary and alternative medicine : eCAM · 2017Article
- Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of FProceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Breakthroughs in the development of antibiotics, antifungals and antiparasitics targeting the pathogens' respiratory chain.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The F1FO-ATP synthase is the only enzyme in nature endowed with bi-functional catalytic mechanism of synthesis and hydrolysis of ATP. The enzyme functions, not only confined to energy transduction, are tied to three intrinsic features of the annular arrangement of c subunits which constitutes the so-called c-ring, the core of the membrane-embedded FO domain: (i) the c-ring constitution is linked to the number of ions (H(+) or Na(+)) channeled across the membrane during the dissipation of the transmembrane electrochemical gradient, which in turn determines the species-specific bioenergetic cost of ATP, the "molecular currency unit" of energy transfer in all living beings; (ii) the c-ring is increasingly involved in the mitochondrial permeability transition, an event linked to cell death and to most mitochondrial dysfunctions; (iii) the c subunit species-specific amino acid sequence and susceptibility to post-translational modifications can address antibacterial drug design according to the model of enzyme inhibitors which target the c subunits. Therefore, the simple c-ring structure not only allows the F1FO-ATP synthase to perform the two opposite tasks of molecular machine of cell life and death, but it also amplifies the enzyme's potential role as a drug target.
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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.