ReviewFrontiers in microbiology2022
CryoEM Reveals the Complexity and Diversity of ATP Synthases.
Review in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 41 citations in OpenAlex.
- Article
- Design, Synthesis, and Biological Evaluation of Mono- and Diamino-Substituted Squaramide Derivatives as Potent Inhibitors of Mycobacterial Adenosine Triphosphate (ATP) Synthase.Journal of medicinal chemistry · 2025Article
- Structures of rotary ATP synthase fromScience advances · 2025Article
- Structural dynamics of mitochondrial ATP synthase inbioRxiv : the preprint server for biology · 2025Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Structure of yeast RAVE bound to a partial VProceedings of the National Academy of Sciences of the United States of America · 2024Article
- ATP synthase subunit ATP5B interacts with TGEV Nsp2 and acts as a negative regulator of TGEV replication.Virulence · 2024Article
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- Structure, Regulation, and Significance of Cyanobacterial and Chloroplast Adenosine Triphosphate Synthase in the Adaptability of Oxygenic Photosynthetic Organisms.Microorganisms · 2024Review
- Directed proton transfer from FBiophysical reviews · 2023Review
- A tale of two inhibitors: diarylquinolines and squaramides.The EMBO journal · 2023Article
- Mechanism of mycobacterial ATP synthase inhibition by squaramides and second generation diarylquinolines.The EMBO journal · 2023Article
- Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase.Nature communications · 2023Article
- FInternational journal of molecular sciences · 2023Review
- Changes within the central stalk of E. coli FCommunications biology · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During respiration, adenosine triphosphate (ATP) synthases harness the electrochemical proton motive force (PMF) generated by the electron transport chain (ETC) to synthesize ATP. These macromolecular machines operate by a remarkable rotary catalytic mechanism that couples transmembrane proton translocation to rotation of a rotor subcomplex, and rotation to ATP synthesis. Initially, x-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cross-linking were the only ways to gain insights into the three-dimensional (3D) structures of ATP synthases and, in particular, provided ground-breaking insights into the soluble parts of the complex that explained the catalytic mechanism by which rotation is coupled to ATP synthesis. In contrast, early electron microscopy was limited to studying the overall shape of the assembly. However, advances in electron cryomicroscopy (cryoEM) have allowed determination of high-resolution structures, including the membrane regions of ATP synthases. These studies revealed the high-resolution structures of the remaining ATP synthase subunits and showed how these subunits work together in the intact macromolecular machine. CryoEM continues to uncover the diversity of ATP synthase structures across species and has begun to show how ATP synthases can be targeted by therapies to treat human diseases.
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Registered trials
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