ReviewScience advances2016
Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.
Review in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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.
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Who cites it
13 citing papers in PubMed.
- Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.The Journal of biological chemistry · 2023Article
- CRISPR/Cas9-mediated gene editing ofFrontiers in plant science · 2023Article
- Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis.Nature communications · 2022Article
- Structure of the dimeric ATP synthase from bovine mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM.Nature structural & molecular biology · 2020Article
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity.eLife · 2018Article
- Lipid environment of membrane proteins in cryo-EM based structural analysis.Biophysical reviews · 2018Review
- Cryo EM structure of intact rotary HNature communications · 2018Article
- The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018Review
- COGcollator: a web server for analysis of distant relationships between homologous protein families.Biology direct · 2017Article
- Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- From molecular chaperones to membrane motors: through the lens of a mass spectrometrist.Biochemical Society transactions · 2017Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electron cryomicroscopy (cryo-EM) has significantly advanced our understanding of molecular structure in biology. Recent innovations in both hardware and software have made cryo-EM a viable alternative for targets that are not amenable to x-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Cryo-EM has even become the method of choice in some situations where x-ray crystallography and NMR spectroscopy are possible but where cryo-EM can determine structures at higher resolution or with less time or effort. Rotary adenosine triphosphatases (ATPases) are crucial to the maintenance of cellular homeostasis. These enzymes couple the synthesis or hydrolysis of adenosine triphosphate to the use or production of a transmembrane electrochemical ion gradient, respectively. However, the membrane-embedded nature and conformational heterogeneity of intact rotary ATPases have prevented their high-resolution structural analysis to date. Recent application of cryo-EM methods to the different types of rotary ATPase has led to sudden advances in understanding the structure and function of these enzymes, revealing significant conformational heterogeneity and characteristic transmembrane α helices that are highly tilted with respect to the membrane. In this Review, we will discuss what has been learned recently about rotary ATPase structure and function, with a particular focus on the vacuolar-type ATPases.
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