ReviewThe Journal of biological chemistry2012
Two ATPases.
Review in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- 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
- Advances of medical nanorobots for future cancer treatments.Journal of hematology & oncology · 2023Review
- Frankenbacteriosis targeting interactions between pathogen and symbiont to control infection in the tick vector.iScience · 2023Article
- Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2019Article
- Control of rotation of the FJournal of bioenergetics and biomembranes · 2018Review
- Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase.International journal of biological macromolecules · 2017Article
- Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 2017Article
- Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase.International journal of biological macromolecules · 2016Article
- Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2016Article
- Revealing the fate of cell surface human P-glycoprotein (ABCB1): The lysosomal degradation pathway.Biochimica et biophysica acta · 2015Article
- Biological messiness vs. biological genius: Mechanistic aspects and roles of protein promiscuity.The Journal of steroid biochemistry and molecular biology · 2015Review
- Article
- Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase.International journal of biological macromolecules · 2015Article
- Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Biochemistry · 2014Article
- ATP synthase: the right size base model for nanomotors in nanomedicine.TheScientificWorldJournal · 2014Review
- Article
- ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.Current medicinal chemistry · 2013Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this article, I reflect on research on two ATPases. The first is F(1)F(0)-ATPase, also known as ATP synthase. It is the terminal enzyme in oxidative phosphorylation and famous as a nanomotor. Early work on mitochondrial enzyme involved purification in large amount, followed by deduction of subunit composition and stoichiometry and determination of molecular sizes of holoenzyme and individual subunits. Later work on Escherichia coli enzyme utilized mutagenesis and optical probes to reveal the molecular mechanism of ATP hydrolysis and detailed facets of catalysis. The second ATPase is P-glycoprotein, which confers multidrug resistance, notably to anticancer drugs, in mammalian cells. Purification of the protein in large quantity allowed detailed characterization of catalysis, formulation of an alternating sites mechanism, and recently, advances in structural characterization.
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What OpenQuestion holds
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.