ReviewBiochemical Society transactions2013
Spotlighting motors and controls of single FoF1-ATP synthase.
Review in Biochemical Society transactions, 2013. 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.
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Who cites it
15 citing papers in PubMed, 40 citations in OpenAlex.
- Single-Molecule Imaging of Integral Membrane Protein Dynamics and Function.Annual review of biophysics · 2024Review
- Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase.Nature communications · 2023Article
- Structure of ATP synthase under strain during catalysis.Nature communications · 2022Article
- FRETboard: Semisupervised classification of FRET traces.Biophysical journal · 2021Article
- Cryo-EM structures provide insight into how E. coli FNature communications · 2020Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018Review
- Toward dynamic structural biology: Two decades of single-molecule Förster resonance energy transfer.Science (New York, N.Y.) · 2018Review
- Visualizing Mitochondrial FFrontiers in physiology · 2018Review
- 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
- F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase.The Journal of biological chemistry · 2015Article
- Inhibition of F1-ATPase rotational catalysis by the carboxyl-terminal domain of the ϵ subunit.The Journal of biological chemistry · 2014Article
- The regulatory switch of FProceedings of SPIE--the International Society for Optical Engineering · 2014Article
- Regulatory conformational changes of the ε subunit in single FRET-labeled FProceedings of SPIE--the International Society for Optical Engineering · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F1 and Fo motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent F1 structure of the Escherichia coli enzyme with the ϵ-subunit in an inhibitory conformation initiated a study for real-time monitoring of the conformational changes of ϵ. The present mini-review summarizes smFRET rotation experiments and previews new smFRET data on the conformational changes of the CTD (C-terminal domain) of ϵ in the E. coli enzyme.
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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.