Genetic Fusions of Globular Proteins to the ε Subunit of theEscherichia coli ATP Synthase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference59 articles.
1. THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE
2. ROTATIONAL COUPLING IN THE F0F1 ATP SYNTHASE
3. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
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1. Evidence for a Partially Stalled γ Rotor in F1-ATPase from Hydrogen–Deuterium Exchange Experiments and Molecular Dynamics Simulations;Journal of the American Chemical Society;2018-10-19
2. 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
3. ATP synthase from Escherichia coli : Mechanism of rotational catalysis, and inhibition with the ε subunit and phytopolyphenols;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2016-02
4. Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase;Journal of Biological Chemistry;2015-08
5. Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit;Journal of Biological Chemistry;2014-10
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