ArticleThe Journal of biological chemistry2019
Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed, 5 citations in OpenAlex.
- nce-miR-12220 is a vital regulator for microsporidian to infect honeybee via positive modulation of ATP-A and γ-tubulin genes.PLoS pathogens · 2026Article
- Deciphering the enigma of RNA editing in the ATP1_alpha subunit of ATP synthase inSaudi journal of biological sciences · 2023Article
- Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its FCell death and differentiation · 2022Article
- The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2021Article
- Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2019Article
- Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase.Biochimica et biophysica acta. Bioenergetics · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ATP synthase uses a rotary mechanism to couple transmembrane proton translocation to ATP synthesis and hydrolysis, which occur at the catalytic sites in the β subunits. In the presence of Mg
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Identifiers
What OpenQuestion holds
Registered trials
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