The ϵ subunit of bacterial and chloroplast F1F0 ATPases
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference30 articles.
1. Coupling between catalytic sites and the proton channel in F1F0-type ATPases
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5. ATP synthase's second stalk comes into focus
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1. Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IF1 Subunits of the F1FO-ATPase as Related to the Endosymbiotic Origin of Mitochondria;Microorganisms;2022-07-07
2. Control of rotation of the F1FO-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF1 proteins;Journal of Bioenergetics and Biomembranes;2018-09-28
3. Unidirectional regulation of the F1FO-ATP synthase nanomotor by the ζ pawl-ratchet inhibitor protein of Paracoccus denitrificans and related α-proteobacteria;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2018-09
4. Acetylation and phosphorylation control both local and global stability of the chloroplast F1 ATP synthase;Scientific Reports;2017-03-09
5. Modulation of coupling in the Escherichia coli ATP synthase by ADP and P i : Role of the ε subunit C-terminal domain;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2017-01
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