ReviewFrontiers in physiology2018
The Peripheral Stalk of Rotary ATPases.
Review in Frontiers in physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A New Perspective on the Role of Alterations in Mitochondrial Proteins Involved in ATP Synthesis and Mobilization in Cardiomyopathies.International journal of molecular sciences · 2025Review
- Differential Expression of Nuclear-Encoded Mitochondrial Protein Genes of ATP Synthase Across Different Tissues of Female Buffalo.Molecular biotechnology · 2025Article
- Review
- Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023Review
- Structural and functional understanding of disease-associated mutations in V-ATPase subunit a1 and other isoforms.Frontiers in molecular neuroscience · 2023Review
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- From the Structural and (Dys)Function of ATP Synthase to Deficiency in Age-Related Diseases.Life (Basel, Switzerland) · 2022Review
- Evolutionary rate covariation identifies SLC30A9 (ZnT9) as a mitochondrial zinc transporter.The Biochemical journal · 2021Article
- Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.PloS one · 2021Article
- Reversible Thiol Oxidation Inhibits the Mitochondrial ATP Synthase inAntioxidants (Basel, Switzerland) · 2020Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Mitochondrial F-ATP Synthase and Its Transition into an Energy-Dissipating Molecular Machine.Oxidative medicine and cellular longevity · 2019Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotary ATPases are a family of enzymes that are thought of as molecular nanomotors and are classified in three types: F, A, and V-type ATPases. Two members (F and A-type) can synthesize and hydrolyze ATP, depending on the energetic needs of the cell, while the V-type enzyme exhibits only a hydrolytic activity. The overall architecture of all these enzymes is conserved and three main sectors are distinguished: a catalytic core, a rotor and a stator or peripheral stalk. The peripheral stalks of the A and V-types are highly conserved in both structure and function, however, the F-type peripheral stalks have divergent structures. Furthermore, the peripheral stalk has other roles beyond its stator function, as evidenced by several biochemical and recent structural studies. This review describes the information regarding the organization of the peripheral stalk components of F, A, and V-ATPases, highlighting the key differences between the studied enzymes, as well as the different processes in which the structure is involved.
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